Manganese in PDB 7klk: Human ARGINASE1 Complexed with Inhibitor Compound 3A
Enzymatic activity of Human ARGINASE1 Complexed with Inhibitor Compound 3A
All present enzymatic activity of Human ARGINASE1 Complexed with Inhibitor Compound 3A:
3.5.3.1;
Protein crystallography data
The structure of Human ARGINASE1 Complexed with Inhibitor Compound 3A, PDB code: 7klk
was solved by
R.L.Palte,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
67.08 /
1.80
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
53.157,
281.463,
67.078,
90,
90.06,
90
|
|
R / Rfree (%)
|
20.5 /
23.7
|
Manganese Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Manganese atom in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
(pdb code 7klk). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the
Human ARGINASE1 Complexed with Inhibitor Compound 3A, PDB code: 7klk:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Manganese binding site 1 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 1 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn401
b:8.0
occ:1.00
|
OD2
|
A:ASP124
|
2.1
|
7.9
|
1.0
|
|
ND1
|
A:HIS101
|
2.2
|
8.6
|
1.0
|
|
OD2
|
A:ASP232
|
2.2
|
10.1
|
1.0
|
|
OD2
|
A:ASP128
|
2.2
|
10.4
|
1.0
|
|
O1
|
A:XFP403
|
2.4
|
12.8
|
1.0
|
|
O
|
A:XFP403
|
2.5
|
13.1
|
1.0
|
|
CG
|
A:ASP124
|
3.0
|
8.1
|
1.0
|
|
B
|
A:XFP403
|
3.0
|
13.2
|
1.0
|
|
CG
|
A:ASP232
|
3.1
|
9.2
|
1.0
|
|
CG
|
A:ASP128
|
3.1
|
10.6
|
1.0
|
|
CG
|
A:HIS101
|
3.2
|
7.8
|
1.0
|
|
CE1
|
A:HIS101
|
3.2
|
8.5
|
1.0
|
|
MN
|
A:MN402
|
3.3
|
8.7
|
1.0
|
|
OD1
|
A:ASP124
|
3.3
|
8.6
|
1.0
|
|
OD1
|
A:ASP128
|
3.4
|
10.3
|
1.0
|
|
CB
|
A:HIS101
|
3.4
|
5.8
|
1.0
|
|
CB
|
A:ASP232
|
3.5
|
8.1
|
1.0
|
|
O2
|
A:XFP403
|
3.7
|
13.8
|
1.0
|
|
OD1
|
A:ASP232
|
4.3
|
9.0
|
1.0
|
|
C7
|
A:XFP403
|
4.3
|
13.1
|
1.0
|
|
NE2
|
A:HIS101
|
4.3
|
9.4
|
1.0
|
|
CD2
|
A:HIS101
|
4.3
|
8.6
|
1.0
|
|
NE1
|
A:TRP122
|
4.3
|
10.0
|
1.0
|
|
CB
|
A:ASP124
|
4.4
|
6.4
|
1.0
|
|
CB
|
A:ASP128
|
4.5
|
9.7
|
1.0
|
|
O
|
A:HIS141
|
4.6
|
9.8
|
1.0
|
|
CZ2
|
A:TRP122
|
4.6
|
10.1
|
1.0
|
|
CE2
|
A:TRP122
|
4.8
|
9.7
|
1.0
|
|
CG
|
A:GLU277
|
4.8
|
9.9
|
1.0
|
|
OE2
|
A:GLU277
|
4.8
|
14.9
|
1.0
|
|
CA
|
A:ASP232
|
4.8
|
7.4
|
1.0
|
|
CA
|
A:HIS101
|
4.9
|
6.8
|
1.0
|
|
OD1
|
A:ASP234
|
4.9
|
6.2
|
1.0
|
|
OD2
|
A:ASP234
|
5.0
|
7.2
|
1.0
|
|
Manganese binding site 2 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 2 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn402
b:8.7
occ:1.00
|
O
|
A:XFP403
|
2.1
|
13.1
|
1.0
|
|
OD2
|
A:ASP234
|
2.1
|
7.2
|
1.0
|
|
OD1
|
A:ASP124
|
2.1
|
8.6
|
1.0
|
|
OD2
|
A:ASP232
|
2.2
|
10.1
|
1.0
|
|
ND1
|
A:HIS126
|
2.3
|
10.1
|
1.0
|
|
OD1
|
A:ASP234
|
2.3
|
6.2
|
1.0
|
|
CG
|
A:ASP234
|
2.5
|
5.6
|
1.0
|
|
O2
|
A:XFP403
|
2.7
|
13.8
|
1.0
|
|
B
|
A:XFP403
|
3.0
|
13.2
|
1.0
|
|
CG
|
A:ASP232
|
3.0
|
9.2
|
1.0
|
|
CG
|
A:ASP124
|
3.1
|
8.1
|
1.0
|
|
CE1
|
A:HIS126
|
3.2
|
10.9
|
1.0
|
|
MN
|
A:MN401
|
3.3
|
8.0
|
1.0
|
|
CG
|
A:HIS126
|
3.4
|
10.0
|
1.0
|
|
OD2
|
A:ASP124
|
3.5
|
7.9
|
1.0
|
|
OD1
|
A:ASP232
|
3.5
|
9.0
|
1.0
|
|
O1
|
A:XFP403
|
3.7
|
12.8
|
1.0
|
|
CB
|
A:HIS126
|
3.8
|
8.2
|
1.0
|
|
OG1
|
A:THR246
|
3.9
|
15.2
|
1.0
|
|
CB
|
A:ASP234
|
4.0
|
6.2
|
1.0
|
|
CB
|
A:ASP232
|
4.1
|
8.1
|
1.0
|
|
C7
|
A:XFP403
|
4.2
|
13.1
|
1.0
|
|
N
|
A:HIS126
|
4.2
|
7.6
|
1.0
|
|
N
|
A:ALA125
|
4.3
|
6.4
|
1.0
|
|
NE2
|
A:HIS126
|
4.4
|
11.8
|
1.0
|
|
CB
|
A:ASP124
|
4.5
|
6.4
|
1.0
|
|
CD2
|
A:HIS126
|
4.5
|
11.0
|
1.0
|
|
C6
|
A:XFP403
|
4.5
|
13.4
|
1.0
|
|
OD1
|
A:ASP128
|
4.5
|
10.3
|
1.0
|
|
CA
|
A:HIS126
|
4.7
|
8.1
|
1.0
|
|
O
|
A:HOH540
|
4.7
|
8.8
|
1.0
|
|
CB
|
A:ALA125
|
4.8
|
7.8
|
1.0
|
|
OD2
|
A:ASP128
|
4.8
|
10.4
|
1.0
|
|
CA
|
A:ASP124
|
4.9
|
5.5
|
1.0
|
|
CA
|
A:ASP234
|
5.0
|
6.2
|
1.0
|
|
CA
|
A:ALA125
|
5.0
|
7.3
|
1.0
|
|
Manganese binding site 3 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 3 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn401
b:9.3
occ:1.00
|
OD2
|
B:ASP124
|
2.1
|
12.7
|
1.0
|
|
OD2
|
B:ASP128
|
2.2
|
8.2
|
1.0
|
|
O2
|
B:XFP403
|
2.2
|
15.8
|
1.0
|
|
O1
|
B:XFP403
|
2.2
|
14.2
|
1.0
|
|
ND1
|
B:HIS101
|
2.3
|
11.0
|
1.0
|
|
OD2
|
B:ASP232
|
2.3
|
7.7
|
1.0
|
|
B
|
B:XFP403
|
2.9
|
15.5
|
1.0
|
|
CG
|
B:ASP124
|
3.0
|
11.0
|
1.0
|
|
CG
|
B:ASP128
|
3.1
|
6.3
|
1.0
|
|
CG
|
B:HIS101
|
3.2
|
10.5
|
1.0
|
|
CE1
|
B:HIS101
|
3.3
|
11.6
|
1.0
|
|
MN
|
B:MN402
|
3.3
|
8.4
|
1.0
|
|
CG
|
B:ASP232
|
3.3
|
7.9
|
1.0
|
|
OD1
|
B:ASP124
|
3.3
|
10.1
|
1.0
|
|
OD1
|
B:ASP128
|
3.4
|
8.1
|
1.0
|
|
CB
|
B:HIS101
|
3.5
|
8.8
|
1.0
|
|
CB
|
B:ASP232
|
3.6
|
8.1
|
1.0
|
|
O
|
B:XFP403
|
3.6
|
16.0
|
1.0
|
|
O
|
B:HOH501
|
3.8
|
13.5
|
1.0
|
|
C7
|
B:XFP403
|
4.2
|
16.1
|
1.0
|
|
NE1
|
B:TRP122
|
4.3
|
10.9
|
1.0
|
|
OD1
|
B:ASP232
|
4.4
|
7.0
|
1.0
|
|
CD2
|
B:HIS101
|
4.4
|
10.9
|
1.0
|
|
NE2
|
B:HIS101
|
4.4
|
12.0
|
1.0
|
|
CB
|
B:ASP124
|
4.4
|
8.8
|
1.0
|
|
CB
|
B:ASP128
|
4.5
|
6.7
|
1.0
|
|
O
|
B:HIS141
|
4.5
|
11.5
|
1.0
|
|
CZ2
|
B:TRP122
|
4.6
|
9.6
|
1.0
|
|
CE2
|
B:TRP122
|
4.8
|
9.8
|
1.0
|
|
CG
|
B:GLU277
|
4.8
|
6.4
|
1.0
|
|
OE2
|
B:GLU277
|
4.9
|
12.5
|
1.0
|
|
ND1
|
B:HIS126
|
4.9
|
10.5
|
1.0
|
|
OD2
|
B:ASP234
|
5.0
|
11.8
|
1.0
|
|
CA
|
B:HIS101
|
5.0
|
8.2
|
1.0
|
|
CB
|
B:HIS126
|
5.0
|
8.8
|
1.0
|
|
Manganese binding site 4 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 4 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn402
b:8.4
occ:1.00
|
O1
|
B:XFP403
|
2.0
|
14.2
|
1.0
|
|
ND1
|
B:HIS126
|
2.1
|
10.5
|
1.0
|
|
OD1
|
B:ASP124
|
2.1
|
10.1
|
1.0
|
|
OD2
|
B:ASP234
|
2.2
|
11.8
|
1.0
|
|
OD2
|
B:ASP232
|
2.2
|
7.7
|
1.0
|
|
OD1
|
B:ASP234
|
2.4
|
8.0
|
1.0
|
|
CG
|
B:ASP234
|
2.6
|
7.4
|
1.0
|
|
O
|
B:XFP403
|
2.7
|
16.0
|
1.0
|
|
B
|
B:XFP403
|
2.9
|
15.5
|
1.0
|
|
CE1
|
B:HIS126
|
3.0
|
11.3
|
1.0
|
|
CG
|
B:ASP232
|
3.1
|
7.9
|
1.0
|
|
CG
|
B:ASP124
|
3.1
|
11.0
|
1.0
|
|
MN
|
B:MN401
|
3.3
|
9.3
|
1.0
|
|
CG
|
B:HIS126
|
3.3
|
9.3
|
1.0
|
|
OD2
|
B:ASP124
|
3.5
|
12.7
|
1.0
|
|
OD1
|
B:ASP232
|
3.6
|
7.0
|
1.0
|
|
O2
|
B:XFP403
|
3.6
|
15.8
|
1.0
|
|
CB
|
B:HIS126
|
3.7
|
8.8
|
1.0
|
|
N
|
B:HIS126
|
4.1
|
8.2
|
1.0
|
|
OG1
|
B:THR246
|
4.1
|
18.2
|
1.0
|
|
CB
|
B:ASP232
|
4.1
|
8.1
|
1.0
|
|
CB
|
B:ASP234
|
4.1
|
5.6
|
1.0
|
|
C7
|
B:XFP403
|
4.2
|
16.1
|
1.0
|
|
NE2
|
B:HIS126
|
4.2
|
11.7
|
1.0
|
|
N
|
B:ALA125
|
4.3
|
6.6
|
1.0
|
|
CD2
|
B:HIS126
|
4.3
|
10.9
|
1.0
|
|
C6
|
B:XFP403
|
4.4
|
17.0
|
1.0
|
|
CB
|
B:ASP124
|
4.5
|
8.8
|
1.0
|
|
OD1
|
B:ASP128
|
4.5
|
8.1
|
1.0
|
|
CA
|
B:HIS126
|
4.6
|
8.7
|
1.0
|
|
O
|
B:HOH517
|
4.7
|
10.1
|
1.0
|
|
CB
|
B:ALA125
|
4.8
|
8.1
|
1.0
|
|
OD2
|
B:ASP128
|
4.8
|
8.2
|
1.0
|
|
CA
|
B:ASP124
|
4.9
|
7.1
|
1.0
|
|
C
|
B:ALA125
|
4.9
|
8.1
|
1.0
|
|
CA
|
B:ALA125
|
4.9
|
7.6
|
1.0
|
|
Manganese binding site 5 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 5 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn401
b:8.6
occ:1.00
|
O2
|
C:XFP404
|
2.0
|
11.3
|
1.0
|
|
OD1
|
C:ASP124
|
2.1
|
6.8
|
1.0
|
|
ND1
|
C:HIS126
|
2.2
|
11.5
|
1.0
|
|
OD2
|
C:ASP234
|
2.3
|
10.7
|
1.0
|
|
OD1
|
C:ASP234
|
2.4
|
7.7
|
1.0
|
|
OD2
|
C:ASP232
|
2.4
|
7.1
|
1.0
|
|
CG
|
C:ASP234
|
2.7
|
8.4
|
1.0
|
|
O1
|
C:XFP404
|
2.7
|
12.4
|
1.0
|
|
B
|
C:XFP404
|
3.0
|
11.7
|
1.0
|
|
CG
|
C:ASP124
|
3.0
|
7.6
|
1.0
|
|
CE1
|
C:HIS126
|
3.1
|
12.0
|
1.0
|
|
CG
|
C:ASP232
|
3.1
|
5.5
|
1.0
|
|
MN
|
C:MN402
|
3.3
|
9.6
|
1.0
|
|
CG
|
C:HIS126
|
3.3
|
10.4
|
1.0
|
|
OD2
|
C:ASP124
|
3.4
|
9.3
|
1.0
|
|
OD1
|
C:ASP232
|
3.6
|
6.4
|
1.0
|
|
CB
|
C:HIS126
|
3.7
|
8.8
|
1.0
|
|
O
|
C:XFP404
|
3.8
|
11.6
|
1.0
|
|
OG1
|
C:THR246
|
4.1
|
16.0
|
1.0
|
|
CB
|
C:ASP232
|
4.1
|
6.8
|
1.0
|
|
CB
|
C:ASP234
|
4.2
|
6.9
|
1.0
|
|
C7
|
C:XFP404
|
4.2
|
11.8
|
1.0
|
|
N
|
C:HIS126
|
4.2
|
7.2
|
1.0
|
|
N
|
C:ALA125
|
4.3
|
7.3
|
1.0
|
|
NE2
|
C:HIS126
|
4.3
|
12.2
|
1.0
|
|
CB
|
C:ASP124
|
4.4
|
7.4
|
1.0
|
|
CD2
|
C:HIS126
|
4.4
|
11.7
|
1.0
|
|
OD1
|
C:ASP128
|
4.5
|
11.9
|
1.0
|
|
C6
|
C:XFP404
|
4.5
|
12.3
|
1.0
|
|
O
|
C:HOH523
|
4.6
|
9.4
|
1.0
|
|
CA
|
C:HIS126
|
4.6
|
7.8
|
1.0
|
|
OD2
|
C:ASP128
|
4.8
|
9.4
|
1.0
|
|
CA
|
C:ASP124
|
4.8
|
7.1
|
1.0
|
|
CB
|
C:ALA125
|
4.9
|
8.5
|
1.0
|
|
CA
|
C:ALA125
|
4.9
|
7.8
|
1.0
|
|
C
|
C:ALA125
|
5.0
|
7.8
|
1.0
|
|
C
|
C:ASP124
|
5.0
|
8.1
|
1.0
|
|
Manganese binding site 6 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 6 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn402
b:9.6
occ:1.00
|
OD2
|
C:ASP124
|
2.0
|
9.3
|
1.0
|
|
ND1
|
C:HIS101
|
2.1
|
5.1
|
1.0
|
|
OD2
|
C:ASP128
|
2.1
|
9.4
|
1.0
|
|
OD2
|
C:ASP232
|
2.3
|
7.1
|
1.0
|
|
O2
|
C:XFP404
|
2.4
|
11.3
|
1.0
|
|
O
|
C:XFP404
|
2.5
|
11.6
|
1.0
|
|
B
|
C:XFP404
|
3.0
|
11.7
|
1.0
|
|
CG
|
C:ASP124
|
3.0
|
7.6
|
1.0
|
|
CG
|
C:ASP128
|
3.1
|
9.1
|
1.0
|
|
CE1
|
C:HIS101
|
3.1
|
4.2
|
1.0
|
|
CG
|
C:HIS101
|
3.1
|
3.4
|
1.0
|
|
MN
|
C:MN401
|
3.3
|
8.6
|
1.0
|
|
CG
|
C:ASP232
|
3.3
|
5.5
|
1.0
|
|
OD1
|
C:ASP128
|
3.4
|
11.9
|
1.0
|
|
OD1
|
C:ASP124
|
3.4
|
6.8
|
1.0
|
|
CB
|
C:HIS101
|
3.4
|
5.2
|
1.0
|
|
CB
|
C:ASP232
|
3.7
|
6.8
|
1.0
|
|
O1
|
C:XFP404
|
3.8
|
12.4
|
1.0
|
|
NE2
|
C:HIS101
|
4.2
|
3.0
|
1.0
|
|
C7
|
C:XFP404
|
4.2
|
11.8
|
1.0
|
|
CD2
|
C:HIS101
|
4.3
|
3.8
|
1.0
|
|
CB
|
C:ASP124
|
4.4
|
7.4
|
1.0
|
|
CB
|
C:ASP128
|
4.4
|
6.5
|
1.0
|
|
NE1
|
C:TRP122
|
4.4
|
10.2
|
1.0
|
|
OD1
|
C:ASP232
|
4.4
|
6.4
|
1.0
|
|
O
|
C:HIS141
|
4.6
|
9.5
|
1.0
|
|
CZ2
|
C:TRP122
|
4.6
|
10.4
|
1.0
|
|
CG
|
C:GLU277
|
4.8
|
13.1
|
1.0
|
|
OE2
|
C:GLU277
|
4.8
|
11.6
|
1.0
|
|
CE2
|
C:TRP122
|
4.9
|
9.8
|
1.0
|
|
ND1
|
C:HIS126
|
4.9
|
11.5
|
1.0
|
|
CA
|
C:HIS101
|
4.9
|
6.1
|
1.0
|
|
OD2
|
C:ASP234
|
5.0
|
10.7
|
1.0
|
|
CB
|
C:HIS126
|
5.0
|
8.8
|
1.0
|
|
Manganese binding site 7 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 7 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 7 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn401
b:7.9
occ:1.00
|
OD2
|
D:ASP124
|
2.1
|
6.9
|
1.0
|
|
O1
|
D:XFP403
|
2.1
|
11.6
|
1.0
|
|
OD2
|
D:ASP128
|
2.1
|
9.1
|
1.0
|
|
OD2
|
D:ASP232
|
2.1
|
8.2
|
1.0
|
|
ND1
|
D:HIS101
|
2.3
|
9.0
|
1.0
|
|
O2
|
D:XFP403
|
2.6
|
13.3
|
1.0
|
|
B
|
D:XFP403
|
3.0
|
12.8
|
1.0
|
|
CG
|
D:ASP124
|
3.0
|
8.6
|
1.0
|
|
CG
|
D:ASP128
|
3.0
|
9.2
|
1.0
|
|
CG
|
D:ASP232
|
3.2
|
9.4
|
1.0
|
|
OD1
|
D:ASP124
|
3.2
|
10.9
|
1.0
|
|
CG
|
D:HIS101
|
3.2
|
8.1
|
1.0
|
|
OD1
|
D:ASP128
|
3.2
|
9.8
|
1.0
|
|
MN
|
D:MN402
|
3.3
|
10.4
|
1.0
|
|
CE1
|
D:HIS101
|
3.3
|
9.5
|
1.0
|
|
CB
|
D:HIS101
|
3.4
|
8.1
|
1.0
|
|
CB
|
D:ASP232
|
3.5
|
8.4
|
1.0
|
|
O
|
D:XFP403
|
3.6
|
12.1
|
1.0
|
|
OD1
|
D:ASP232
|
4.3
|
7.6
|
1.0
|
|
C7
|
D:XFP403
|
4.3
|
14.1
|
1.0
|
|
NE1
|
D:TRP122
|
4.3
|
9.3
|
1.0
|
|
CB
|
D:ASP124
|
4.3
|
5.8
|
1.0
|
|
CD2
|
D:HIS101
|
4.4
|
8.8
|
1.0
|
|
NE2
|
D:HIS101
|
4.4
|
9.7
|
1.0
|
|
CB
|
D:ASP128
|
4.4
|
7.3
|
1.0
|
|
O
|
D:HIS141
|
4.6
|
10.9
|
1.0
|
|
CZ2
|
D:TRP122
|
4.6
|
9.3
|
1.0
|
|
CG
|
D:GLU277
|
4.8
|
10.3
|
1.0
|
|
CE2
|
D:TRP122
|
4.8
|
9.0
|
1.0
|
|
OE2
|
D:GLU277
|
4.8
|
11.7
|
1.0
|
|
ND1
|
D:HIS126
|
4.9
|
8.6
|
1.0
|
|
CB
|
D:HIS126
|
4.9
|
6.8
|
1.0
|
|
CA
|
D:ASP232
|
4.9
|
8.5
|
1.0
|
|
CA
|
D:HIS101
|
5.0
|
7.9
|
1.0
|
|
OD1
|
D:ASP234
|
5.0
|
8.0
|
1.0
|
|
OD2
|
D:ASP234
|
5.0
|
8.1
|
1.0
|
|
Manganese binding site 8 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 8 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 8 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mn402
b:10.4
occ:1.00
|
OD1
|
D:ASP124
|
2.0
|
10.9
|
1.0
|
|
OD2
|
D:ASP234
|
2.1
|
8.1
|
1.0
|
|
ND1
|
D:HIS126
|
2.2
|
8.6
|
1.0
|
|
O1
|
D:XFP403
|
2.2
|
11.6
|
1.0
|
|
OD2
|
D:ASP232
|
2.3
|
8.2
|
1.0
|
|
OD1
|
D:ASP234
|
2.4
|
8.0
|
1.0
|
|
CG
|
D:ASP234
|
2.6
|
7.8
|
1.0
|
|
O
|
D:XFP403
|
2.8
|
12.1
|
1.0
|
|
CE1
|
D:HIS126
|
3.1
|
9.8
|
1.0
|
|
CG
|
D:ASP232
|
3.1
|
9.4
|
1.0
|
|
CG
|
D:ASP124
|
3.1
|
8.6
|
1.0
|
|
B
|
D:XFP403
|
3.1
|
12.8
|
1.0
|
|
CG
|
D:HIS126
|
3.3
|
7.7
|
1.0
|
|
MN
|
D:MN401
|
3.3
|
7.9
|
1.0
|
|
OD2
|
D:ASP124
|
3.5
|
6.9
|
1.0
|
|
OD1
|
D:ASP232
|
3.6
|
7.6
|
1.0
|
|
CB
|
D:HIS126
|
3.6
|
6.8
|
1.0
|
|
O2
|
D:XFP403
|
4.0
|
13.3
|
1.0
|
|
CB
|
D:ASP234
|
4.1
|
5.8
|
1.0
|
|
CB
|
D:ASP232
|
4.1
|
8.4
|
1.0
|
|
OG1
|
D:THR246
|
4.2
|
16.2
|
1.0
|
|
N
|
D:ALA125
|
4.2
|
6.2
|
1.0
|
|
N
|
D:HIS126
|
4.2
|
8.8
|
1.0
|
|
C7
|
D:XFP403
|
4.2
|
14.1
|
1.0
|
|
NE2
|
D:HIS126
|
4.3
|
9.7
|
1.0
|
|
CD2
|
D:HIS126
|
4.4
|
8.6
|
1.0
|
|
CB
|
D:ASP124
|
4.4
|
5.8
|
1.0
|
|
OD1
|
D:ASP128
|
4.4
|
9.8
|
1.0
|
|
C6
|
D:XFP403
|
4.5
|
15.3
|
1.0
|
|
O
|
D:HOH553
|
4.5
|
13.7
|
1.0
|
|
CA
|
D:HIS126
|
4.6
|
8.0
|
1.0
|
|
CA
|
D:ASP124
|
4.8
|
5.6
|
1.0
|
|
OD2
|
D:ASP128
|
4.8
|
9.1
|
1.0
|
|
CB
|
D:ALA125
|
4.9
|
8.3
|
1.0
|
|
CA
|
D:ALA125
|
5.0
|
8.3
|
1.0
|
|
C
|
D:ASP124
|
5.0
|
6.3
|
1.0
|
|
C
|
D:ALA125
|
5.0
|
8.8
|
1.0
|
|
CA
|
D:ASP234
|
5.0
|
6.6
|
1.0
|
|
Manganese binding site 9 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 9 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 9 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn401
b:13.8
occ:1.00
|
OD2
|
E:ASP124
|
2.1
|
12.6
|
1.0
|
|
OD2
|
E:ASP128
|
2.1
|
10.2
|
1.0
|
|
ND1
|
E:HIS101
|
2.2
|
18.7
|
1.0
|
|
O2
|
E:XFP403
|
2.2
|
18.0
|
1.0
|
|
OD2
|
E:ASP232
|
2.3
|
15.4
|
1.0
|
|
O1
|
E:XFP403
|
2.5
|
18.7
|
1.0
|
|
B
|
E:XFP403
|
3.0
|
18.5
|
1.0
|
|
CG
|
E:ASP128
|
3.1
|
9.8
|
1.0
|
|
CG
|
E:ASP124
|
3.1
|
14.1
|
1.0
|
|
CG
|
E:HIS101
|
3.1
|
16.9
|
1.0
|
|
CE1
|
E:HIS101
|
3.2
|
19.3
|
1.0
|
|
CG
|
E:ASP232
|
3.2
|
15.2
|
1.0
|
|
MN
|
E:MN402
|
3.3
|
12.7
|
1.0
|
|
OD1
|
E:ASP128
|
3.4
|
10.3
|
1.0
|
|
CB
|
E:HIS101
|
3.4
|
14.0
|
1.0
|
|
OD1
|
E:ASP124
|
3.5
|
14.6
|
1.0
|
|
CB
|
E:ASP232
|
3.6
|
12.0
|
1.0
|
|
O
|
E:XFP403
|
3.8
|
18.8
|
1.0
|
|
C7
|
E:XFP403
|
4.2
|
18.3
|
1.0
|
|
CD2
|
E:HIS101
|
4.3
|
17.8
|
1.0
|
|
OD1
|
E:ASP232
|
4.3
|
16.6
|
1.0
|
|
NE2
|
E:HIS101
|
4.3
|
19.2
|
1.0
|
|
O
|
E:HIS141
|
4.4
|
17.7
|
1.0
|
|
CB
|
E:ASP124
|
4.4
|
11.9
|
1.0
|
|
NE1
|
E:TRP122
|
4.4
|
14.1
|
1.0
|
|
CB
|
E:ASP128
|
4.5
|
9.9
|
1.0
|
|
CZ2
|
E:TRP122
|
4.5
|
14.2
|
1.0
|
|
CE2
|
E:TRP122
|
4.8
|
13.7
|
1.0
|
|
CG
|
E:GLU277
|
4.9
|
16.5
|
1.0
|
|
CA
|
E:HIS101
|
4.9
|
13.8
|
1.0
|
|
OE2
|
E:GLU277
|
5.0
|
18.1
|
1.0
|
|
CA
|
E:ASP232
|
5.0
|
11.7
|
1.0
|
|
CB
|
E:HIS126
|
5.0
|
11.5
|
1.0
|
|
Manganese binding site 10 out
of 12 in 7klk
Go back to
Manganese Binding Sites List in 7klk
Manganese binding site 10 out
of 12 in the Human ARGINASE1 Complexed with Inhibitor Compound 3A
 Mono view
 Stereo pair view
|
|
A full contact list of Manganese with other atoms in the Mn binding
site number 10 of Human ARGINASE1 Complexed with Inhibitor Compound 3A within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mn402
b:12.7
occ:1.00
|
OD2
|
E:ASP232
|
2.1
|
15.4
|
1.0
|
|
O2
|
E:XFP403
|
2.1
|
18.0
|
1.0
|
|
OD1
|
E:ASP124
|
2.2
|
14.6
|
1.0
|
|
OD2
|
E:ASP234
|
2.3
|
16.0
|
1.0
|
|
ND1
|
E:HIS126
|
2.3
|
13.9
|
1.0
|
|
OD1
|
E:ASP234
|
2.4
|
14.6
|
1.0
|
|
CG
|
E:ASP234
|
2.6
|
13.9
|
1.0
|
|
O
|
E:XFP403
|
2.8
|
18.8
|
1.0
|
|
CG
|
E:ASP232
|
3.0
|
15.2
|
1.0
|
|
B
|
E:XFP403
|
3.1
|
18.5
|
1.0
|
|
CG
|
E:ASP124
|
3.1
|
14.1
|
1.0
|
|
CE1
|
E:HIS126
|
3.2
|
14.4
|
1.0
|
|
MN
|
E:MN401
|
3.3
|
13.8
|
1.0
|
|
CG
|
E:HIS126
|
3.4
|
12.3
|
1.0
|
|
OD2
|
E:ASP124
|
3.4
|
12.6
|
1.0
|
|
OD1
|
E:ASP232
|
3.6
|
16.6
|
1.0
|
|
CB
|
E:HIS126
|
3.7
|
11.5
|
1.0
|
|
O1
|
E:XFP403
|
3.9
|
18.7
|
1.0
|
|
OG1
|
E:THR246
|
4.0
|
20.7
|
1.0
|
|
CB
|
E:ASP232
|
4.1
|
12.0
|
1.0
|
|
CB
|
E:ASP234
|
4.1
|
11.8
|
1.0
|
|
C7
|
E:XFP403
|
4.2
|
18.3
|
1.0
|
|
N
|
E:HIS126
|
4.2
|
10.1
|
1.0
|
|
N
|
E:ALA125
|
4.3
|
9.7
|
1.0
|
|
NE2
|
E:HIS126
|
4.4
|
14.7
|
1.0
|
|
CB
|
E:ASP124
|
4.4
|
11.9
|
1.0
|
|
CD2
|
E:HIS126
|
4.5
|
13.6
|
1.0
|
|
O
|
E:HOH506
|
4.6
|
20.9
|
1.0
|
|
C6
|
E:XFP403
|
4.6
|
18.2
|
1.0
|
|
OD1
|
E:ASP128
|
4.6
|
10.3
|
1.0
|
|
CA
|
E:HIS126
|
4.6
|
10.9
|
1.0
|
|
OD2
|
E:ASP128
|
4.8
|
10.2
|
1.0
|
|
CA
|
E:ASP124
|
4.9
|
10.6
|
1.0
|
|
CB
|
E:ALA125
|
4.9
|
9.5
|
1.0
|
|
CA
|
E:ALA125
|
5.0
|
10.0
|
1.0
|
|
Reference:
M.Lu,
H.Zhang,
D.Li,
M.Childers,
Q.Pu,
R.L.Palte,
S.Gathiaka,
T.W.Lyons,
A.Palani,
P.W.Fan,
P.Spacciapoli,
J.R.Miller,
H.Cho,
M.Cheng,
K.Chakravarthy,
J.O'neil,
P.Eangoor,
A.Beard,
H.Y.Kim,
J.Sauri,
H.Gunaydin,
D.L.Sloman,
P.Siliphaivanh,
J.Cumming,
C.Fischer.
Structure-Based Discovery of Proline-Derived Arginase Inhibitors with Improved Oral Bioavailability For Immuno-Oncology. Acs Med.Chem.Lett. V. 12 1380 2021.
ISSN: ISSN 1948-5875
PubMed: 34527178
DOI: 10.1021/ACSMEDCHEMLETT.1C00195
Page generated: Sun Oct 6 09:21:38 2024
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