Manganese in PDB 1hq5: Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue
Enzymatic activity of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue
All present enzymatic activity of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue:
3.5.3.1;
Protein crystallography data
The structure of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue, PDB code: 1hq5
was solved by
N.N.Kim,
J.D.Cox,
R.F.Baggio,
F.A.Emig,
S.K.Mistry,
S.L.Harper,
D.W.Speicher,
S.M.Morris Jr.,
D.E.Ash,
A.Traish,
D.W.Christianson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.30
|
Space group
|
P 3
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.300,
91.300,
69.400,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
15.8 /
19.4
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue
(pdb code 1hq5). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the
Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue, PDB code: 1hq5:
Jump to Manganese binding site number:
1;
2;
3;
4;
Manganese binding site 1 out
of 4 in 1hq5
Go back to
Manganese Binding Sites List in 1hq5
Manganese binding site 1 out
of 4 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn500
b:28.6
occ:1.00
|
OD2
|
A:ASP124
|
2.1
|
13.5
|
1.0
|
OD2
|
A:ASP128
|
2.1
|
12.2
|
1.0
|
OD2
|
A:ASP232
|
2.2
|
17.7
|
1.0
|
O3
|
A:S2C551
|
2.2
|
30.2
|
1.0
|
ND1
|
A:HIS101
|
2.2
|
23.2
|
1.0
|
O1
|
A:S2C551
|
2.5
|
28.3
|
1.0
|
B
|
A:S2C551
|
2.8
|
30.7
|
1.0
|
CG
|
A:HIS101
|
3.1
|
23.2
|
1.0
|
CG
|
A:ASP128
|
3.2
|
13.3
|
1.0
|
CG
|
A:ASP124
|
3.2
|
13.9
|
1.0
|
CB
|
A:HIS101
|
3.3
|
22.5
|
1.0
|
O2
|
A:S2C551
|
3.3
|
31.6
|
1.0
|
CE1
|
A:HIS101
|
3.3
|
22.7
|
1.0
|
CG
|
A:ASP232
|
3.3
|
17.4
|
1.0
|
MN
|
A:MN501
|
3.4
|
22.3
|
1.0
|
OD1
|
A:ASP128
|
3.5
|
10.9
|
1.0
|
OD1
|
A:ASP124
|
3.8
|
12.5
|
1.0
|
CB
|
A:ASP232
|
3.8
|
18.6
|
1.0
|
O
|
A:HIS141
|
4.1
|
16.8
|
1.0
|
CE
|
A:S2C551
|
4.2
|
32.5
|
1.0
|
CD2
|
A:HIS101
|
4.3
|
22.2
|
1.0
|
NE2
|
A:HIS101
|
4.3
|
20.3
|
1.0
|
OD1
|
A:ASP232
|
4.4
|
18.9
|
1.0
|
NE1
|
A:TRP122
|
4.4
|
16.1
|
1.0
|
CB
|
A:ASP124
|
4.4
|
13.9
|
1.0
|
CB
|
A:ASP128
|
4.5
|
12.7
|
1.0
|
CZ2
|
A:TRP122
|
4.6
|
17.6
|
1.0
|
CG
|
A:GLU277
|
4.7
|
19.7
|
1.0
|
CD
|
A:S2C551
|
4.7
|
35.3
|
1.0
|
CA
|
A:HIS101
|
4.8
|
22.8
|
1.0
|
CE2
|
A:TRP122
|
4.9
|
16.6
|
1.0
|
OE2
|
A:GLU277
|
4.9
|
20.5
|
1.0
|
|
Manganese binding site 2 out
of 4 in 1hq5
Go back to
Manganese Binding Sites List in 1hq5
Manganese binding site 2 out
of 4 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn501
b:22.3
occ:1.00
|
OD1
|
A:ASP124
|
2.1
|
12.5
|
1.0
|
O3
|
A:S2C551
|
2.2
|
30.2
|
1.0
|
OD2
|
A:ASP234
|
2.3
|
18.6
|
1.0
|
OD1
|
A:ASP234
|
2.4
|
16.7
|
1.0
|
ND1
|
A:HIS126
|
2.5
|
13.6
|
1.0
|
CG
|
A:ASP234
|
2.7
|
20.0
|
1.0
|
O2
|
A:S2C551
|
2.7
|
31.6
|
1.0
|
OD2
|
A:ASP232
|
2.7
|
17.7
|
1.0
|
CG
|
A:ASP124
|
2.9
|
13.9
|
1.0
|
B
|
A:S2C551
|
3.0
|
30.7
|
1.0
|
OD2
|
A:ASP124
|
3.1
|
13.5
|
1.0
|
CG
|
A:ASP232
|
3.2
|
17.4
|
1.0
|
CE1
|
A:HIS126
|
3.3
|
11.7
|
1.0
|
MN
|
A:MN500
|
3.4
|
28.6
|
1.0
|
CG
|
A:HIS126
|
3.6
|
12.1
|
1.0
|
OD1
|
A:ASP232
|
3.6
|
18.9
|
1.0
|
CE
|
A:S2C551
|
3.8
|
32.5
|
1.0
|
CB
|
A:HIS126
|
3.9
|
12.6
|
1.0
|
CB
|
A:ASP232
|
4.0
|
18.6
|
1.0
|
N
|
A:HIS126
|
4.1
|
13.4
|
1.0
|
N
|
A:ALA125
|
4.1
|
14.8
|
1.0
|
O1
|
A:S2C551
|
4.1
|
28.3
|
1.0
|
CB
|
A:ASP234
|
4.2
|
17.9
|
1.0
|
CB
|
A:ASP124
|
4.3
|
13.9
|
1.0
|
CD
|
A:S2C551
|
4.3
|
35.3
|
1.0
|
NE2
|
A:HIS126
|
4.5
|
12.7
|
1.0
|
CA
|
A:HIS126
|
4.6
|
12.2
|
1.0
|
CD2
|
A:HIS126
|
4.6
|
12.7
|
1.0
|
O
|
A:HOH614
|
4.7
|
12.5
|
1.0
|
CA
|
A:ASP124
|
4.7
|
15.2
|
1.0
|
OD1
|
A:ASP128
|
4.7
|
10.9
|
1.0
|
CB
|
A:ALA125
|
4.8
|
13.2
|
1.0
|
C
|
A:ALA125
|
4.8
|
13.7
|
1.0
|
CA
|
A:ALA125
|
4.8
|
13.5
|
1.0
|
OD2
|
A:ASP128
|
4.8
|
12.2
|
1.0
|
C
|
A:ASP124
|
4.9
|
14.9
|
1.0
|
O
|
A:THR246
|
4.9
|
23.0
|
1.0
|
C
|
A:ASP234
|
5.0
|
16.2
|
1.0
|
O
|
A:ASP234
|
5.0
|
16.8
|
1.0
|
|
Manganese binding site 3 out
of 4 in 1hq5
Go back to
Manganese Binding Sites List in 1hq5
Manganese binding site 3 out
of 4 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn502
b:27.1
occ:1.00
|
OD2
|
B:ASP124
|
2.1
|
19.6
|
1.0
|
OD2
|
B:ASP128
|
2.1
|
13.7
|
1.0
|
OD2
|
B:ASP232
|
2.1
|
21.2
|
1.0
|
O3
|
B:S2C552
|
2.2
|
20.0
|
1.0
|
ND1
|
B:HIS101
|
2.2
|
11.7
|
1.0
|
O1
|
B:S2C552
|
2.5
|
20.1
|
1.0
|
B
|
B:S2C552
|
2.8
|
19.6
|
1.0
|
CG
|
B:HIS101
|
3.1
|
11.5
|
1.0
|
CG
|
B:ASP128
|
3.2
|
14.1
|
1.0
|
CB
|
B:HIS101
|
3.3
|
12.8
|
1.0
|
CG
|
B:ASP124
|
3.3
|
15.2
|
1.0
|
O2
|
B:S2C552
|
3.3
|
18.7
|
1.0
|
CG
|
B:ASP232
|
3.3
|
18.9
|
1.0
|
CE1
|
B:HIS101
|
3.3
|
13.7
|
1.0
|
MN
|
B:MN503
|
3.4
|
18.6
|
1.0
|
OD1
|
B:ASP128
|
3.5
|
12.3
|
1.0
|
OD1
|
B:ASP124
|
3.8
|
10.2
|
1.0
|
CB
|
B:ASP232
|
3.8
|
18.4
|
1.0
|
O
|
B:HIS141
|
4.1
|
13.2
|
1.0
|
CE
|
B:S2C552
|
4.2
|
20.7
|
1.0
|
CD2
|
B:HIS101
|
4.3
|
9.6
|
1.0
|
OD1
|
B:ASP232
|
4.3
|
19.0
|
1.0
|
NE2
|
B:HIS101
|
4.3
|
9.2
|
1.0
|
NE1
|
B:TRP122
|
4.4
|
16.2
|
1.0
|
CB
|
B:ASP124
|
4.5
|
16.3
|
1.0
|
CB
|
B:ASP128
|
4.5
|
15.7
|
1.0
|
CZ2
|
B:TRP122
|
4.6
|
18.1
|
1.0
|
CG
|
B:GLU277
|
4.7
|
17.5
|
1.0
|
CD
|
B:S2C552
|
4.7
|
22.7
|
1.0
|
CA
|
B:HIS101
|
4.8
|
14.3
|
1.0
|
CE2
|
B:TRP122
|
4.9
|
16.7
|
1.0
|
OE2
|
B:GLU277
|
4.9
|
15.9
|
1.0
|
|
Manganese binding site 4 out
of 4 in 1hq5
Go back to
Manganese Binding Sites List in 1hq5
Manganese binding site 4 out
of 4 in the Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Crystal Structure of the Binuclear Manganese Metalloenzyme Arginase Complexed with S-(2-Boronoethyl)-L-Cysteine, An L-Arginine Analogue within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn503
b:18.6
occ:1.00
|
OD1
|
B:ASP124
|
2.1
|
10.2
|
1.0
|
O3
|
B:S2C552
|
2.2
|
20.0
|
1.0
|
OD2
|
B:ASP234
|
2.3
|
16.7
|
1.0
|
OD1
|
B:ASP234
|
2.4
|
14.6
|
1.0
|
ND1
|
B:HIS126
|
2.5
|
15.1
|
1.0
|
O2
|
B:S2C552
|
2.7
|
18.7
|
1.0
|
CG
|
B:ASP234
|
2.7
|
14.3
|
1.0
|
OD2
|
B:ASP232
|
2.8
|
21.2
|
1.0
|
CG
|
B:ASP124
|
2.9
|
15.2
|
1.0
|
B
|
B:S2C552
|
3.0
|
19.6
|
1.0
|
OD2
|
B:ASP124
|
3.1
|
19.6
|
1.0
|
CG
|
B:ASP232
|
3.2
|
18.9
|
1.0
|
CE1
|
B:HIS126
|
3.3
|
13.0
|
1.0
|
MN
|
B:MN502
|
3.4
|
27.1
|
1.0
|
CG
|
B:HIS126
|
3.6
|
14.2
|
1.0
|
OD1
|
B:ASP232
|
3.6
|
19.0
|
1.0
|
CE
|
B:S2C552
|
3.8
|
20.7
|
1.0
|
CB
|
B:HIS126
|
4.0
|
14.1
|
1.0
|
CB
|
B:ASP232
|
4.1
|
18.4
|
1.0
|
N
|
B:ALA125
|
4.1
|
13.5
|
1.0
|
N
|
B:HIS126
|
4.1
|
14.1
|
1.0
|
O1
|
B:S2C552
|
4.1
|
20.1
|
1.0
|
CB
|
B:ASP234
|
4.2
|
13.5
|
1.0
|
CB
|
B:ASP124
|
4.3
|
16.3
|
1.0
|
CD
|
B:S2C552
|
4.3
|
22.7
|
1.0
|
NE2
|
B:HIS126
|
4.5
|
13.8
|
1.0
|
CD2
|
B:HIS126
|
4.6
|
13.4
|
1.0
|
CA
|
B:HIS126
|
4.6
|
14.0
|
1.0
|
CA
|
B:ASP124
|
4.7
|
15.8
|
1.0
|
OD1
|
B:ASP128
|
4.7
|
12.3
|
1.0
|
CB
|
B:ALA125
|
4.7
|
11.7
|
1.0
|
CA
|
B:ALA125
|
4.8
|
13.1
|
1.0
|
C
|
B:ALA125
|
4.8
|
13.6
|
1.0
|
OD2
|
B:ASP128
|
4.8
|
13.7
|
1.0
|
C
|
B:ASP124
|
4.9
|
15.4
|
1.0
|
O
|
B:THR246
|
4.9
|
19.4
|
1.0
|
C
|
B:ASP234
|
5.0
|
14.7
|
1.0
|
O
|
B:ASP234
|
5.0
|
17.0
|
1.0
|
|
Reference:
N.N.Kim,
J.D.Cox,
R.F.Baggio,
F.A.Emig,
S.K.Mistry,
S.L.Harper,
D.W.Speicher,
S.M.Morris Jr.,
D.E.Ash,
A.Traish,
D.W.Christianson.
Probing Erectile Function: S-(2-Boronoethyl)-L-Cysteine Binds to Arginase As A Transition State Analogue and Enhances Smooth Muscle Relaxation in Human Penile Corpus Cavernosum. Biochemistry V. 40 2678 2001.
ISSN: ISSN 0006-2960
PubMed: 11258879
DOI: 10.1021/BI002317H
Page generated: Sat Oct 5 10:54:01 2024
|