Zinc in PDB 5ld9: Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1.
Protein crystallography data
The structure of Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1., PDB code: 5ld9
was solved by
J.A.Maupin-Furlow,
B.Franzetti,
S.Cao,
E.Girard,
F.Gabel,
S.Engilberge,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
25.39 /
1.73
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
34.202,
37.147,
60.131,
97.29,
104.18,
100.07
|
R / Rfree (%)
|
15.7 /
18.9
|
Other elements in 5ld9:
The structure of Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1.
(pdb code 5ld9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1., PDB code: 5ld9:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 5ld9
Go back to
Zinc Binding Sites List in 5ld9
Zinc binding site 1 out
of 2 in the Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn201
b:24.8
occ:0.90
|
OD2
|
A:ASP101
|
2.0
|
15.8
|
1.0
|
NE2
|
A:HIS90
|
2.0
|
18.2
|
1.0
|
NE2
|
A:HIS88
|
2.0
|
16.8
|
1.0
|
O
|
A:HOH360
|
2.1
|
19.9
|
1.0
|
CG
|
A:ASP101
|
2.7
|
17.0
|
1.0
|
OD1
|
A:ASP101
|
2.7
|
18.6
|
1.0
|
CD2
|
A:HIS90
|
2.9
|
18.1
|
1.0
|
CD2
|
A:HIS88
|
3.0
|
17.1
|
1.0
|
HD2
|
A:HIS90
|
3.0
|
21.7
|
1.0
|
CE1
|
A:HIS88
|
3.0
|
21.9
|
1.0
|
CE1
|
A:HIS90
|
3.1
|
18.9
|
1.0
|
HD2
|
A:HIS88
|
3.2
|
20.5
|
1.0
|
HE1
|
A:HIS88
|
3.2
|
26.3
|
1.0
|
HE1
|
A:HIS90
|
3.4
|
22.7
|
1.0
|
H
|
A:SER98
|
3.6
|
19.5
|
1.0
|
HG
|
A:SER98
|
3.8
|
23.4
|
1.0
|
HD13
|
A:ILE114
|
3.8
|
22.4
|
1.0
|
HB3
|
A:SER98
|
3.9
|
26.1
|
1.0
|
HE1
|
A:PHE62
|
3.9
|
21.8
|
1.0
|
OG
|
A:SER98
|
3.9
|
19.5
|
1.0
|
O
|
A:HOH354
|
4.0
|
37.8
|
1.0
|
CG
|
A:HIS90
|
4.1
|
15.7
|
1.0
|
ND1
|
A:HIS88
|
4.1
|
16.2
|
1.0
|
CB
|
A:ASP101
|
4.1
|
14.5
|
1.0
|
CG
|
A:HIS88
|
4.2
|
17.3
|
1.0
|
ND1
|
A:HIS90
|
4.2
|
15.9
|
1.0
|
HD1
|
A:PHE62
|
4.2
|
21.9
|
1.0
|
HB2
|
A:ASP101
|
4.4
|
17.4
|
1.0
|
CB
|
A:SER98
|
4.4
|
21.7
|
1.0
|
HG23
|
A:ILE114
|
4.4
|
21.0
|
1.0
|
HA
|
A:PRO97
|
4.4
|
18.2
|
1.0
|
HG21
|
A:ILE114
|
4.4
|
21.0
|
1.0
|
N
|
A:SER98
|
4.5
|
16.2
|
1.0
|
OE1
|
A:GLU34
|
4.5
|
20.0
|
1.0
|
O
|
A:HOH339
|
4.5
|
28.5
|
1.0
|
HB3
|
A:ASP101
|
4.5
|
17.4
|
1.0
|
O
|
A:HOH377
|
4.6
|
27.3
|
1.0
|
CE1
|
A:PHE62
|
4.7
|
18.2
|
1.0
|
CD1
|
A:ILE114
|
4.7
|
18.7
|
1.0
|
OE2
|
A:GLU34
|
4.7
|
21.8
|
1.0
|
HD11
|
A:ILE114
|
4.7
|
22.4
|
1.0
|
CD1
|
A:PHE62
|
4.8
|
18.2
|
1.0
|
CG2
|
A:ILE114
|
4.9
|
17.5
|
1.0
|
H
|
A:ASP101
|
4.9
|
23.5
|
1.0
|
HG12
|
A:ILE114
|
4.9
|
16.7
|
1.0
|
HZ3
|
A:TRP112
|
4.9
|
23.1
|
1.0
|
CD
|
A:GLU34
|
5.0
|
20.3
|
1.0
|
O
|
A:SER89
|
5.0
|
18.2
|
1.0
|
|
Zinc binding site 2 out
of 2 in 5ld9
Go back to
Zinc Binding Sites List in 5ld9
Zinc binding site 2 out
of 2 in the Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1.
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of Deubiquitinating Enzyme Homolog, Pyrococcus Furiosus JAMM1. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn201
b:27.9
occ:0.90
|
OD2
|
B:ASP101
|
1.9
|
23.4
|
1.0
|
NE2
|
B:HIS90
|
2.0
|
21.4
|
1.0
|
NE2
|
B:HIS88
|
2.0
|
18.9
|
1.0
|
O
|
B:HOH357
|
2.1
|
23.1
|
1.0
|
CG
|
B:ASP101
|
2.6
|
18.8
|
1.0
|
OD1
|
B:ASP101
|
2.6
|
19.3
|
1.0
|
CD2
|
B:HIS90
|
2.9
|
22.8
|
1.0
|
HD2
|
B:HIS90
|
3.0
|
27.4
|
1.0
|
CD2
|
B:HIS88
|
3.0
|
22.2
|
1.0
|
CE1
|
B:HIS88
|
3.0
|
22.1
|
1.0
|
CE1
|
B:HIS90
|
3.1
|
24.9
|
1.0
|
HD2
|
B:HIS88
|
3.2
|
26.6
|
1.0
|
HE1
|
B:HIS88
|
3.2
|
26.5
|
1.0
|
HE1
|
B:HIS90
|
3.4
|
29.8
|
1.0
|
H
|
B:SER98
|
3.7
|
23.2
|
1.0
|
HD13
|
B:ILE114
|
3.8
|
26.5
|
1.0
|
O
|
B:HOH343
|
3.8
|
36.3
|
1.0
|
HE1
|
B:PHE62
|
4.0
|
28.4
|
1.0
|
HG
|
B:SER98
|
4.0
|
24.6
|
1.0
|
CG
|
B:HIS90
|
4.1
|
18.1
|
1.0
|
CB
|
B:ASP101
|
4.1
|
21.4
|
1.0
|
OG
|
B:SER98
|
4.1
|
20.5
|
1.0
|
ND1
|
B:HIS88
|
4.1
|
17.9
|
1.0
|
CG
|
B:HIS88
|
4.2
|
19.2
|
1.0
|
ND1
|
B:HIS90
|
4.2
|
22.1
|
1.0
|
O
|
B:HOH337
|
4.2
|
39.3
|
1.0
|
HB3
|
B:SER98
|
4.2
|
29.6
|
1.0
|
HA
|
B:PRO97
|
4.4
|
25.4
|
1.0
|
HB2
|
B:ASP101
|
4.4
|
25.7
|
1.0
|
HG23
|
B:ILE114
|
4.4
|
24.9
|
1.0
|
OE1
|
B:GLU34
|
4.4
|
25.8
|
1.0
|
HB3
|
B:ASP101
|
4.4
|
25.7
|
1.0
|
HD1
|
B:PHE62
|
4.4
|
26.1
|
1.0
|
HG21
|
B:ILE114
|
4.4
|
24.9
|
1.0
|
O
|
B:HOH379
|
4.5
|
38.3
|
1.0
|
OE2
|
B:GLU34
|
4.5
|
27.2
|
1.0
|
N
|
B:SER98
|
4.6
|
19.4
|
1.0
|
CB
|
B:SER98
|
4.7
|
24.7
|
1.0
|
CD1
|
B:ILE114
|
4.7
|
22.1
|
1.0
|
HD11
|
B:ILE114
|
4.7
|
26.5
|
1.0
|
CE1
|
B:PHE62
|
4.8
|
23.6
|
1.0
|
CD
|
B:GLU34
|
4.8
|
24.1
|
1.0
|
CG2
|
B:ILE114
|
4.9
|
20.8
|
1.0
|
O
|
B:HOH314
|
4.9
|
33.3
|
1.0
|
HG12
|
B:ILE114
|
4.9
|
26.8
|
1.0
|
O
|
B:SER89
|
4.9
|
21.5
|
1.0
|
HZ3
|
B:TRP112
|
5.0
|
23.4
|
1.0
|
|
Reference:
S.Cao,
S.Engilberge,
E.Girard,
F.Gabel,
B.Franzetti,
J.A.Maupin-Furlow.
Structural Insight Into Ubiquitin-Like Protein Recognition and Oligomeric States of Jamm/Mpn(+) Proteases. Structure V. 25 823 2017.
ISSN: ISSN 1878-4186
PubMed: 28479062
DOI: 10.1016/J.STR.2017.04.002
Page generated: Sun Oct 27 20:57:10 2024
|