Zinc in PDB 3p1v: Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution
Protein crystallography data
The structure of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution, PDB code: 3p1v
was solved by
Joint Center For Structural Genomics (Jcsg),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.91 /
1.93
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
72.919,
84.963,
139.758,
90.00,
99.56,
90.00
|
R / Rfree (%)
|
17 /
20.7
|
Other elements in 3p1v:
The structure of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution
(pdb code 3p1v). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution, PDB code: 3p1v:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 3p1v
Go back to
Zinc Binding Sites List in 3p1v
Zinc binding site 1 out
of 4 in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn426
b:25.9
occ:0.60
|
O2
|
A:PO4433
|
1.9
|
55.5
|
1.0
|
OD1
|
A:ASP322
|
2.0
|
21.1
|
1.0
|
NE2
|
A:HIS315
|
2.1
|
20.4
|
1.0
|
NE2
|
A:HIS311
|
2.2
|
22.2
|
1.0
|
P
|
A:PO4433
|
2.5
|
52.5
|
1.0
|
O1
|
A:PO4433
|
2.7
|
56.1
|
1.0
|
O3
|
A:PO4433
|
2.8
|
61.0
|
1.0
|
CG
|
A:ASP322
|
2.8
|
22.1
|
1.0
|
OD2
|
A:ASP322
|
2.9
|
24.2
|
1.0
|
CE1
|
A:HIS315
|
3.1
|
20.5
|
1.0
|
CD2
|
A:HIS311
|
3.1
|
22.4
|
1.0
|
CD2
|
A:HIS315
|
3.1
|
20.6
|
1.0
|
CE1
|
A:HIS311
|
3.2
|
22.1
|
1.0
|
O4
|
A:PO4433
|
4.0
|
60.4
|
1.0
|
OE1
|
A:GLU312
|
4.1
|
30.4
|
1.0
|
CB
|
A:ASP322
|
4.2
|
21.5
|
1.0
|
ND1
|
A:HIS315
|
4.2
|
21.7
|
1.0
|
CG
|
A:HIS315
|
4.2
|
20.5
|
1.0
|
CG
|
A:HIS311
|
4.2
|
21.5
|
1.0
|
ND1
|
A:HIS311
|
4.3
|
23.3
|
1.0
|
OH
|
A:TYR324
|
4.4
|
27.5
|
1.0
|
CE2
|
A:TYR324
|
4.4
|
22.9
|
1.0
|
CE
|
A:MSE400
|
4.5
|
15.5
|
1.0
|
O
|
A:HOH854
|
4.7
|
42.6
|
1.0
|
CA
|
A:ASP322
|
4.8
|
20.6
|
1.0
|
CZ
|
A:TYR324
|
4.9
|
26.6
|
1.0
|
CD
|
A:GLU312
|
4.9
|
31.0
|
1.0
|
|
Zinc binding site 2 out
of 4 in 3p1v
Go back to
Zinc Binding Sites List in 3p1v
Zinc binding site 2 out
of 4 in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn427
b:21.8
occ:1.00
|
OE2
|
A:GLU323
|
2.0
|
21.1
|
1.0
|
SG
|
A:CYS412
|
2.3
|
20.1
|
1.0
|
SG
|
A:CYS409
|
2.4
|
22.6
|
1.0
|
SG
|
A:CYS398
|
2.4
|
21.1
|
1.0
|
CD
|
A:GLU323
|
2.9
|
19.5
|
1.0
|
OE1
|
A:GLU323
|
3.2
|
24.4
|
1.0
|
CB
|
A:CYS412
|
3.2
|
17.4
|
1.0
|
CB
|
A:CYS398
|
3.4
|
17.6
|
1.0
|
CB
|
A:CYS409
|
3.4
|
19.4
|
1.0
|
N
|
A:CYS409
|
3.8
|
20.5
|
1.0
|
CA
|
A:CYS409
|
4.2
|
20.7
|
1.0
|
N
|
A:CYS412
|
4.2
|
21.6
|
1.0
|
ND2
|
A:ASN345
|
4.2
|
18.6
|
1.0
|
CA
|
A:CYS412
|
4.2
|
19.8
|
1.0
|
CG
|
A:GLU323
|
4.3
|
20.0
|
1.0
|
CB
|
A:MSE400
|
4.3
|
15.4
|
1.0
|
CB
|
A:ASN345
|
4.4
|
19.6
|
1.0
|
CG
|
A:MSE400
|
4.4
|
17.6
|
1.0
|
CD
|
A:PRO394
|
4.6
|
23.1
|
1.0
|
O
|
A:CYS409
|
4.8
|
23.3
|
1.0
|
C
|
A:CYS409
|
4.8
|
25.1
|
1.0
|
CA
|
A:CYS398
|
4.8
|
19.2
|
1.0
|
CG
|
A:ASN345
|
4.8
|
31.3
|
1.0
|
CG
|
A:PRO394
|
4.8
|
27.6
|
1.0
|
C
|
A:PHE408
|
5.0
|
24.6
|
1.0
|
N
|
A:MSE400
|
5.0
|
17.3
|
1.0
|
|
Zinc binding site 3 out
of 4 in 3p1v
Go back to
Zinc Binding Sites List in 3p1v
Zinc binding site 3 out
of 4 in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn426
b:68.7
occ:0.50
|
OD1
|
B:ASP322
|
2.2
|
67.0
|
1.0
|
NE2
|
B:HIS315
|
2.2
|
54.4
|
1.0
|
O
|
B:HOH546
|
2.2
|
55.8
|
1.0
|
NE2
|
B:HIS311
|
2.2
|
57.1
|
1.0
|
CG
|
B:ASP322
|
2.9
|
66.7
|
1.0
|
OD2
|
B:ASP322
|
3.0
|
74.3
|
1.0
|
CD2
|
B:HIS311
|
3.1
|
56.8
|
1.0
|
CD2
|
B:HIS315
|
3.1
|
53.1
|
1.0
|
CE1
|
B:HIS315
|
3.2
|
53.7
|
1.0
|
CE1
|
B:HIS311
|
3.3
|
58.3
|
1.0
|
OE1
|
B:GLU312
|
3.8
|
60.7
|
1.0
|
CG
|
B:HIS311
|
4.3
|
56.7
|
1.0
|
CG
|
B:HIS315
|
4.3
|
49.8
|
1.0
|
OH
|
B:TYR324
|
4.3
|
77.1
|
1.0
|
ND1
|
B:HIS315
|
4.3
|
52.5
|
1.0
|
ND1
|
B:HIS311
|
4.4
|
59.6
|
1.0
|
CB
|
B:ASP322
|
4.4
|
61.0
|
1.0
|
CE2
|
B:TYR324
|
4.5
|
76.6
|
1.0
|
CE
|
B:MSE400
|
4.6
|
53.3
|
1.0
|
CD
|
B:GLU312
|
4.7
|
69.5
|
1.0
|
CZ
|
B:TYR324
|
4.9
|
82.3
|
1.0
|
OE2
|
B:GLU312
|
4.9
|
72.2
|
1.0
|
CA
|
B:ASP322
|
5.0
|
59.0
|
1.0
|
|
Zinc binding site 4 out
of 4 in 3p1v
Go back to
Zinc Binding Sites List in 3p1v
Zinc binding site 4 out
of 4 in the Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of A Metallo-Endopeptidases (BACOVA_00663) From Bacteroides Ovatus at 1.93 A Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn427
b:60.3
occ:1.00
|
OE2
|
B:GLU323
|
2.2
|
54.6
|
1.0
|
SG
|
B:CYS412
|
2.3
|
58.8
|
1.0
|
SG
|
B:CYS409
|
2.4
|
63.0
|
1.0
|
SG
|
B:CYS398
|
2.5
|
63.5
|
1.0
|
CD
|
B:GLU323
|
3.1
|
73.3
|
1.0
|
CB
|
B:CYS412
|
3.2
|
55.5
|
1.0
|
CB
|
B:CYS398
|
3.2
|
62.5
|
1.0
|
OE1
|
B:GLU323
|
3.2
|
67.8
|
1.0
|
CB
|
B:CYS409
|
3.4
|
61.6
|
1.0
|
N
|
B:CYS409
|
3.8
|
60.4
|
1.0
|
CA
|
B:CYS409
|
4.1
|
61.3
|
1.0
|
N
|
B:CYS412
|
4.2
|
56.3
|
1.0
|
ND2
|
B:ASN345
|
4.2
|
49.6
|
1.0
|
CA
|
B:CYS412
|
4.2
|
54.8
|
1.0
|
CB
|
B:MSE400
|
4.3
|
53.4
|
1.0
|
CB
|
B:ASN345
|
4.4
|
53.2
|
1.0
|
CG
|
B:MSE400
|
4.4
|
55.7
|
1.0
|
CG
|
B:GLU323
|
4.5
|
70.7
|
1.0
|
CA
|
B:CYS398
|
4.7
|
64.8
|
1.0
|
O
|
B:CYS409
|
4.7
|
62.5
|
1.0
|
C
|
B:CYS409
|
4.8
|
64.7
|
1.0
|
CD
|
B:PRO394
|
4.8
|
64.8
|
1.0
|
CG
|
B:ASN345
|
4.9
|
60.9
|
1.0
|
C
|
B:PHE408
|
4.9
|
63.4
|
1.0
|
N
|
B:MSE400
|
4.9
|
57.4
|
1.0
|
CG
|
B:PRO394
|
5.0
|
67.9
|
1.0
|
|
Reference:
Joint Center For Structural Genomics (Jcsg),
Joint Center For Structural Genomics (Jcsg).
N/A N/A.
Page generated: Sat Oct 26 11:15:36 2024
|