Manganese in PDB 1t4s: Arginase-L-Valine Complex
Enzymatic activity of Arginase-L-Valine Complex
All present enzymatic activity of Arginase-L-Valine Complex:
3.5.3.1;
Protein crystallography data
The structure of Arginase-L-Valine Complex, PDB code: 1t4s
was solved by
E.Cama,
S.Pethe,
J.-L.Boucher,
H.Shoufa,
F.A.Emig,
D.E.Ash,
R.E.Viola,
D.Mansuy,
D.W.Christianson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
28.74 /
2.80
|
Space group
|
P 32
|
Cell size a, b, c (Å), α, β, γ (°)
|
87.800,
87.800,
110.500,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
25.8 /
29.2
|
Manganese Binding Sites:
The binding sites of Manganese atom in the Arginase-L-Valine Complex
(pdb code 1t4s). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the
Arginase-L-Valine Complex, PDB code: 1t4s:
Jump to Manganese binding site number:
1;
2;
3;
4;
5;
6;
Manganese binding site 1 out
of 6 in 1t4s
Go back to
Manganese Binding Sites List in 1t4s
Manganese binding site 1 out
of 6 in the Arginase-L-Valine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 1 of Arginase-L-Valine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn500
b:79.0
occ:1.00
|
ND1
|
A:HIS126
|
2.1
|
82.1
|
1.0
|
OD2
|
A:ASP234
|
2.3
|
68.3
|
1.0
|
OD2
|
A:ASP232
|
2.3
|
56.2
|
1.0
|
OD1
|
A:ASP124
|
2.3
|
73.3
|
1.0
|
OD1
|
A:ASP234
|
2.5
|
69.1
|
1.0
|
O
|
A:HOH729
|
2.7
|
97.0
|
1.0
|
CG
|
A:ASP234
|
2.7
|
68.3
|
1.0
|
CE1
|
A:HIS126
|
2.8
|
80.5
|
1.0
|
OD2
|
A:ASP124
|
2.8
|
76.8
|
1.0
|
CG
|
A:ASP124
|
2.8
|
74.8
|
1.0
|
CG
|
A:ASP232
|
3.1
|
58.3
|
1.0
|
MN
|
A:MN501
|
3.1
|
86.4
|
1.0
|
CG
|
A:HIS126
|
3.3
|
81.9
|
1.0
|
OD1
|
A:ASP232
|
3.7
|
56.2
|
1.0
|
CB
|
A:HIS126
|
3.9
|
81.8
|
1.0
|
N
|
A:HIS126
|
4.0
|
77.8
|
1.0
|
N
|
A:ALA125
|
4.0
|
80.5
|
1.0
|
CB
|
A:ASP232
|
4.0
|
58.4
|
1.0
|
NE2
|
A:HIS126
|
4.1
|
79.5
|
1.0
|
CB
|
A:ASP234
|
4.2
|
66.0
|
1.0
|
OD1
|
A:ASP128
|
4.2
|
94.5
|
1.0
|
CB
|
A:ASP124
|
4.2
|
74.6
|
1.0
|
CD2
|
A:HIS126
|
4.3
|
81.0
|
1.0
|
OD2
|
A:ASP128
|
4.4
|
95.8
|
1.0
|
CA
|
A:HIS126
|
4.5
|
80.5
|
1.0
|
OG1
|
A:THR246
|
4.6
|
72.7
|
1.0
|
CA
|
A:ASP124
|
4.7
|
75.8
|
1.0
|
C
|
A:ALA125
|
4.8
|
80.4
|
1.0
|
CB
|
A:ALA125
|
4.8
|
76.3
|
1.0
|
CA
|
A:ALA125
|
4.8
|
80.6
|
1.0
|
CG
|
A:ASP128
|
4.8
|
93.8
|
1.0
|
C
|
A:ASP124
|
4.8
|
77.5
|
1.0
|
ND1
|
A:HIS101
|
5.0
|
83.8
|
1.0
|
|
Manganese binding site 2 out
of 6 in 1t4s
Go back to
Manganese Binding Sites List in 1t4s
Manganese binding site 2 out
of 6 in the Arginase-L-Valine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 2 of Arginase-L-Valine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mn501
b:86.4
occ:1.00
|
OD2
|
A:ASP124
|
2.1
|
76.8
|
1.0
|
OD2
|
A:ASP128
|
2.1
|
95.8
|
1.0
|
ND1
|
A:HIS101
|
2.3
|
83.8
|
1.0
|
OD2
|
A:ASP232
|
2.3
|
56.2
|
1.0
|
O
|
A:HOH729
|
2.4
|
97.0
|
1.0
|
CG
|
A:ASP128
|
3.0
|
93.8
|
1.0
|
MN
|
A:MN500
|
3.1
|
79.0
|
1.0
|
CG
|
A:HIS101
|
3.2
|
83.5
|
1.0
|
OD1
|
A:ASP128
|
3.3
|
94.5
|
1.0
|
CG
|
A:ASP124
|
3.3
|
74.8
|
1.0
|
CE1
|
A:HIS101
|
3.3
|
85.0
|
1.0
|
CB
|
A:HIS101
|
3.3
|
81.9
|
1.0
|
CG
|
A:ASP232
|
3.4
|
58.3
|
1.0
|
CB
|
A:ASP232
|
3.8
|
58.4
|
1.0
|
OD1
|
A:ASP124
|
3.9
|
73.3
|
1.0
|
O
|
A:HIS141
|
4.3
|
91.1
|
1.0
|
CB
|
A:ASP128
|
4.3
|
91.7
|
1.0
|
CD2
|
A:HIS101
|
4.3
|
83.7
|
1.0
|
NE2
|
A:HIS101
|
4.4
|
85.7
|
1.0
|
CB
|
A:ASP124
|
4.4
|
74.6
|
1.0
|
OD1
|
A:ASP232
|
4.5
|
56.2
|
1.0
|
NE1
|
A:TRP122
|
4.5
|
78.6
|
1.0
|
OE2
|
A:GLU277
|
4.6
|
74.0
|
1.0
|
CZ2
|
A:TRP122
|
4.7
|
79.4
|
1.0
|
ND1
|
A:HIS126
|
4.7
|
82.1
|
1.0
|
OD2
|
A:ASP234
|
4.7
|
68.3
|
1.0
|
CG
|
A:GLU277
|
4.8
|
74.8
|
1.0
|
CA
|
A:HIS101
|
4.9
|
76.2
|
1.0
|
CE2
|
A:TRP122
|
5.0
|
78.7
|
1.0
|
OD1
|
A:ASP234
|
5.0
|
69.1
|
1.0
|
|
Manganese binding site 3 out
of 6 in 1t4s
Go back to
Manganese Binding Sites List in 1t4s
Manganese binding site 3 out
of 6 in the Arginase-L-Valine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 3 of Arginase-L-Valine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn502
b:72.5
occ:1.00
|
ND1
|
B:HIS126
|
2.1
|
73.3
|
1.0
|
OD2
|
B:ASP232
|
2.1
|
63.3
|
1.0
|
OD1
|
B:ASP124
|
2.2
|
72.3
|
1.0
|
OD2
|
B:ASP234
|
2.2
|
71.0
|
1.0
|
OD1
|
B:ASP234
|
2.5
|
73.1
|
1.0
|
CG
|
B:ASP234
|
2.7
|
70.8
|
1.0
|
O
|
B:HOH730
|
2.7
|
84.2
|
1.0
|
CE1
|
B:HIS126
|
2.8
|
74.4
|
1.0
|
CG
|
B:ASP124
|
2.8
|
71.3
|
1.0
|
OD2
|
B:ASP124
|
2.9
|
70.6
|
1.0
|
CG
|
B:ASP232
|
3.0
|
64.3
|
1.0
|
MN
|
B:MN503
|
3.1
|
73.8
|
1.0
|
CG
|
B:HIS126
|
3.3
|
74.3
|
1.0
|
OD1
|
B:ASP232
|
3.6
|
63.2
|
1.0
|
CB
|
B:HIS126
|
3.9
|
74.9
|
1.0
|
CB
|
B:ASP232
|
4.0
|
63.0
|
1.0
|
NE2
|
B:HIS126
|
4.0
|
73.9
|
1.0
|
N
|
B:HIS126
|
4.0
|
76.8
|
1.0
|
N
|
B:ALA125
|
4.1
|
75.2
|
1.0
|
CB
|
B:ASP234
|
4.2
|
67.8
|
1.0
|
CB
|
B:ASP124
|
4.2
|
70.1
|
1.0
|
CD2
|
B:HIS126
|
4.3
|
74.2
|
1.0
|
OD1
|
B:ASP128
|
4.3
|
93.1
|
1.0
|
OD2
|
B:ASP128
|
4.5
|
93.9
|
1.0
|
O
|
B:HOH726
|
4.5
|
56.3
|
1.0
|
OG1
|
B:THR246
|
4.5
|
66.5
|
1.0
|
CA
|
B:HIS126
|
4.6
|
78.2
|
1.0
|
CA
|
B:ASP124
|
4.7
|
69.2
|
1.0
|
CB
|
B:ALA125
|
4.8
|
73.6
|
1.0
|
CG
|
B:ASP128
|
4.8
|
92.2
|
1.0
|
CA
|
B:ALA125
|
4.8
|
75.6
|
1.0
|
C
|
B:ALA125
|
4.9
|
76.3
|
1.0
|
C
|
B:ASP124
|
4.9
|
70.8
|
1.0
|
|
Manganese binding site 4 out
of 6 in 1t4s
Go back to
Manganese Binding Sites List in 1t4s
Manganese binding site 4 out
of 6 in the Arginase-L-Valine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 4 of Arginase-L-Valine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mn503
b:73.8
occ:1.00
|
OD2
|
B:ASP124
|
2.1
|
70.6
|
1.0
|
OD2
|
B:ASP128
|
2.2
|
93.9
|
1.0
|
ND1
|
B:HIS101
|
2.3
|
70.0
|
1.0
|
OD2
|
B:ASP232
|
2.3
|
63.3
|
1.0
|
O
|
B:HOH730
|
2.4
|
84.2
|
1.0
|
CG
|
B:ASP128
|
3.1
|
92.2
|
1.0
|
MN
|
B:MN502
|
3.1
|
72.5
|
1.0
|
CG
|
B:HIS101
|
3.2
|
69.0
|
1.0
|
CG
|
B:ASP124
|
3.3
|
71.3
|
1.0
|
CB
|
B:HIS101
|
3.3
|
69.0
|
1.0
|
OD1
|
B:ASP128
|
3.3
|
93.1
|
1.0
|
CG
|
B:ASP232
|
3.4
|
64.3
|
1.0
|
CE1
|
B:HIS101
|
3.4
|
68.7
|
1.0
|
CB
|
B:ASP232
|
3.8
|
63.0
|
1.0
|
OD1
|
B:ASP124
|
3.8
|
72.3
|
1.0
|
O
|
B:HIS141
|
4.3
|
91.5
|
1.0
|
CB
|
B:ASP128
|
4.4
|
89.8
|
1.0
|
CD2
|
B:HIS101
|
4.4
|
67.2
|
1.0
|
CB
|
B:ASP124
|
4.4
|
70.1
|
1.0
|
NE2
|
B:HIS101
|
4.4
|
67.2
|
1.0
|
OD1
|
B:ASP232
|
4.4
|
63.2
|
1.0
|
NE1
|
B:TRP122
|
4.6
|
84.1
|
1.0
|
OE2
|
B:GLU277
|
4.6
|
71.7
|
1.0
|
ND1
|
B:HIS126
|
4.7
|
73.3
|
1.0
|
CZ2
|
B:TRP122
|
4.7
|
85.5
|
1.0
|
OD2
|
B:ASP234
|
4.7
|
71.0
|
1.0
|
CG
|
B:GLU277
|
4.7
|
71.0
|
1.0
|
CA
|
B:HIS101
|
4.8
|
75.2
|
1.0
|
CE2
|
B:TRP122
|
5.0
|
84.2
|
1.0
|
|
Manganese binding site 5 out
of 6 in 1t4s
Go back to
Manganese Binding Sites List in 1t4s
Manganese binding site 5 out
of 6 in the Arginase-L-Valine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 5 of Arginase-L-Valine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn504
b:58.1
occ:1.00
|
ND1
|
C:HIS126
|
2.1
|
71.7
|
1.0
|
OD2
|
C:ASP234
|
2.2
|
65.6
|
1.0
|
OD2
|
C:ASP232
|
2.2
|
48.7
|
1.0
|
OD1
|
C:ASP124
|
2.3
|
72.2
|
1.0
|
OD1
|
C:ASP234
|
2.5
|
61.5
|
1.0
|
CG
|
C:ASP234
|
2.7
|
63.2
|
1.0
|
O
|
C:HOH728
|
2.8
|
37.7
|
1.0
|
CE1
|
C:HIS126
|
2.8
|
73.0
|
1.0
|
CG
|
C:ASP124
|
2.9
|
71.5
|
1.0
|
OD2
|
C:ASP124
|
2.9
|
73.4
|
1.0
|
CG
|
C:ASP232
|
3.0
|
50.7
|
1.0
|
MN
|
C:MN505
|
3.1
|
81.4
|
1.0
|
CG
|
C:HIS126
|
3.4
|
73.2
|
1.0
|
OD1
|
C:ASP232
|
3.6
|
49.4
|
1.0
|
CB
|
C:HIS126
|
3.9
|
73.8
|
1.0
|
N
|
C:HIS126
|
4.0
|
74.2
|
1.0
|
CB
|
C:ASP232
|
4.0
|
52.1
|
1.0
|
NE2
|
C:HIS126
|
4.0
|
72.6
|
1.0
|
N
|
C:ALA125
|
4.0
|
73.2
|
1.0
|
CB
|
C:ASP234
|
4.2
|
59.7
|
1.0
|
CB
|
C:ASP124
|
4.2
|
70.2
|
1.0
|
OD1
|
C:ASP128
|
4.3
|
86.6
|
1.0
|
CD2
|
C:HIS126
|
4.3
|
72.0
|
1.0
|
OG1
|
C:THR246
|
4.5
|
64.8
|
1.0
|
OD2
|
C:ASP128
|
4.5
|
86.4
|
1.0
|
CA
|
C:HIS126
|
4.6
|
75.3
|
1.0
|
CA
|
C:ASP124
|
4.7
|
61.7
|
1.0
|
CB
|
C:ALA125
|
4.8
|
74.8
|
1.0
|
CA
|
C:ALA125
|
4.8
|
74.2
|
1.0
|
C
|
C:ALA125
|
4.8
|
75.2
|
1.0
|
C
|
C:ASP124
|
4.8
|
64.0
|
1.0
|
CG
|
C:ASP128
|
4.9
|
85.3
|
1.0
|
|
Manganese binding site 6 out
of 6 in 1t4s
Go back to
Manganese Binding Sites List in 1t4s
Manganese binding site 6 out
of 6 in the Arginase-L-Valine Complex
Mono view
Stereo pair view
|
A full contact list of Manganese with other atoms in the Mn binding
site number 6 of Arginase-L-Valine Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mn505
b:81.4
occ:1.00
|
OD2
|
C:ASP124
|
2.1
|
73.4
|
1.0
|
OD2
|
C:ASP128
|
2.2
|
86.4
|
1.0
|
OD2
|
C:ASP232
|
2.3
|
48.7
|
1.0
|
O
|
C:HOH728
|
2.3
|
37.7
|
1.0
|
ND1
|
C:HIS101
|
2.3
|
65.8
|
1.0
|
CG
|
C:ASP128
|
3.1
|
85.3
|
1.0
|
MN
|
C:MN504
|
3.1
|
58.1
|
1.0
|
CG
|
C:HIS101
|
3.2
|
67.1
|
1.0
|
CG
|
C:ASP124
|
3.3
|
71.5
|
1.0
|
OD1
|
C:ASP128
|
3.3
|
86.6
|
1.0
|
CB
|
C:HIS101
|
3.3
|
68.2
|
1.0
|
CG
|
C:ASP232
|
3.3
|
50.7
|
1.0
|
CE1
|
C:HIS101
|
3.4
|
67.4
|
1.0
|
CB
|
C:ASP232
|
3.8
|
52.1
|
1.0
|
OD1
|
C:ASP124
|
3.8
|
72.2
|
1.0
|
O
|
C:HIS141
|
4.3
|
92.0
|
1.0
|
CD2
|
C:HIS101
|
4.4
|
65.7
|
1.0
|
CB
|
C:ASP124
|
4.4
|
70.2
|
1.0
|
CB
|
C:ASP128
|
4.4
|
84.6
|
1.0
|
NE2
|
C:HIS101
|
4.4
|
64.9
|
1.0
|
OD1
|
C:ASP232
|
4.4
|
49.4
|
1.0
|
NE1
|
C:TRP122
|
4.6
|
64.3
|
1.0
|
ND1
|
C:HIS126
|
4.7
|
71.7
|
1.0
|
CZ2
|
C:TRP122
|
4.7
|
69.1
|
1.0
|
OE2
|
C:GLU277
|
4.7
|
69.8
|
1.0
|
CG
|
C:GLU277
|
4.8
|
68.9
|
1.0
|
OD2
|
C:ASP234
|
4.8
|
65.6
|
1.0
|
CA
|
C:HIS101
|
4.9
|
74.7
|
1.0
|
OD1
|
C:ASP234
|
5.0
|
61.5
|
1.0
|
CE2
|
C:TRP122
|
5.0
|
67.8
|
1.0
|
|
Reference:
E.Cama,
S.Pethe,
J.-L.Boucher,
S.Han,
F.A.Emig,
D.E.Ash,
R.E.Viola,
D.Mansuy,
D.W.Christianson.
Inhibitor Coordination Interactions in the Binuclear Manganese Cluster of Arginase Biochemistry V. 43 8987 2004.
ISSN: ISSN 0006-2960
PubMed: 15248756
DOI: 10.1021/BI0491705
Page generated: Sat Oct 5 12:28:58 2024
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