Zinc in PDB 4msd: Crystal Structure of Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant
Protein crystallography data
The structure of Crystal Structure of Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant, PDB code: 4msd
was solved by
R.K.Shrestha,
J.A.Ronau,
C.Das,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
33.61 /
1.90
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
58.048,
74.117,
64.865,
90.00,
113.41,
90.00
|
R / Rfree (%)
|
18.8 /
21.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant
(pdb code 4msd). 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 Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant, PDB code: 4msd:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 4msd
Go back to
Zinc Binding Sites List in 4msd
Zinc binding site 1 out
of 4 in the Crystal Structure of Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant
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 Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:16.3
occ:1.00
|
OD2
|
A:ASP354
|
2.0
|
15.5
|
1.0
|
O
|
A:HOH621
|
2.0
|
18.1
|
1.0
|
NE2
|
A:HIS343
|
2.0
|
16.9
|
1.0
|
NE2
|
A:HIS341
|
2.1
|
15.0
|
1.0
|
CG
|
A:ASP354
|
2.7
|
14.7
|
1.0
|
OD1
|
A:ASP354
|
2.8
|
11.5
|
1.0
|
CD2
|
A:HIS343
|
2.9
|
15.1
|
1.0
|
CE1
|
A:HIS341
|
3.1
|
12.6
|
1.0
|
CD2
|
A:HIS341
|
3.1
|
13.2
|
1.0
|
CE1
|
A:HIS343
|
3.1
|
16.8
|
1.0
|
O
|
A:HOH637
|
3.8
|
21.9
|
1.0
|
OE2
|
A:GLU286
|
3.9
|
17.0
|
1.0
|
O
|
A:HOH652
|
3.9
|
25.4
|
1.0
|
OG
|
A:SER351
|
4.0
|
19.5
|
1.0
|
CG
|
A:HIS343
|
4.1
|
18.4
|
1.0
|
CB
|
A:ASP354
|
4.2
|
12.6
|
1.0
|
ND1
|
A:HIS343
|
4.2
|
19.4
|
1.0
|
ND1
|
A:HIS341
|
4.2
|
13.5
|
1.0
|
CG
|
A:HIS341
|
4.2
|
13.6
|
1.0
|
CB
|
A:SER351
|
4.3
|
20.2
|
1.0
|
N
|
A:SER351
|
4.4
|
15.4
|
1.0
|
O
|
A:PHE349
|
4.4
|
17.2
|
1.0
|
OE1
|
A:GLU286
|
4.6
|
15.7
|
1.0
|
CD
|
A:GLU286
|
4.6
|
19.3
|
1.0
|
C1
|
A:EDO505
|
4.6
|
30.7
|
1.0
|
CG1
|
A:VAL372
|
4.8
|
16.9
|
1.0
|
C2
|
A:EDO505
|
4.9
|
25.9
|
1.0
|
|
Zinc binding site 2 out
of 4 in 4msd
Go back to
Zinc Binding Sites List in 4msd
Zinc binding site 2 out
of 4 in the Crystal Structure of Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant
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 Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:20.9
occ:1.00
|
NE2
|
A:HIS406
|
1.9
|
21.9
|
1.0
|
NE2
|
A:HIS404
|
2.0
|
25.3
|
1.0
|
NE2
|
A:HIS356
|
2.0
|
20.1
|
1.0
|
SG
|
A:CYS397
|
2.3
|
22.2
|
1.0
|
CE1
|
A:HIS406
|
2.7
|
22.4
|
1.0
|
CD2
|
A:HIS404
|
2.9
|
25.2
|
1.0
|
CE1
|
A:HIS356
|
3.0
|
21.9
|
1.0
|
CE1
|
A:HIS404
|
3.0
|
28.7
|
1.0
|
CD2
|
A:HIS406
|
3.0
|
23.2
|
1.0
|
CD2
|
A:HIS356
|
3.0
|
25.7
|
1.0
|
CB
|
A:CYS397
|
3.3
|
23.9
|
1.0
|
ND1
|
A:HIS406
|
3.9
|
23.6
|
1.0
|
CG
|
A:HIS406
|
4.0
|
21.9
|
1.0
|
NH2
|
B:ARG398
|
4.1
|
30.0
|
1.0
|
ND1
|
A:HIS404
|
4.1
|
26.9
|
1.0
|
CG
|
A:HIS404
|
4.1
|
25.7
|
1.0
|
ND1
|
A:HIS356
|
4.1
|
22.0
|
1.0
|
CG
|
A:HIS356
|
4.2
|
22.0
|
1.0
|
OG
|
A:SER352
|
4.5
|
24.8
|
1.0
|
CA
|
A:CYS397
|
4.7
|
25.4
|
1.0
|
CD1
|
A:ILE394
|
4.7
|
21.8
|
1.0
|
CZ
|
B:ARG398
|
4.7
|
41.3
|
1.0
|
C
|
A:CYS397
|
4.9
|
30.1
|
1.0
|
O
|
A:CYS397
|
5.0
|
32.5
|
1.0
|
CB
|
A:LYS399
|
5.0
|
31.2
|
1.0
|
|
Zinc binding site 3 out
of 4 in 4msd
Go back to
Zinc Binding Sites List in 4msd
Zinc binding site 3 out
of 4 in the Crystal Structure of Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant
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 Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn501
b:15.2
occ:1.00
|
O
|
B:HOH624
|
1.9
|
12.8
|
1.0
|
OD2
|
B:ASP354
|
1.9
|
14.5
|
1.0
|
NE2
|
B:HIS343
|
2.0
|
13.7
|
1.0
|
NE2
|
B:HIS341
|
2.0
|
11.3
|
1.0
|
CG
|
B:ASP354
|
2.6
|
12.3
|
1.0
|
OD1
|
B:ASP354
|
2.7
|
13.0
|
1.0
|
CD2
|
B:HIS343
|
2.9
|
14.9
|
1.0
|
CE1
|
B:HIS341
|
2.9
|
14.1
|
1.0
|
CE1
|
B:HIS343
|
3.1
|
13.8
|
1.0
|
CD2
|
B:HIS341
|
3.1
|
12.4
|
1.0
|
OE2
|
B:GLU286
|
3.8
|
13.8
|
1.0
|
OG
|
B:SER351
|
3.9
|
15.7
|
1.0
|
O
|
B:HOH656
|
3.9
|
17.1
|
1.0
|
CB
|
B:ASP354
|
4.1
|
12.7
|
1.0
|
CG
|
B:HIS343
|
4.1
|
14.2
|
1.0
|
ND1
|
B:HIS341
|
4.1
|
12.7
|
1.0
|
ND1
|
B:HIS343
|
4.1
|
15.7
|
1.0
|
CG
|
B:HIS341
|
4.2
|
11.7
|
1.0
|
CB
|
B:SER351
|
4.3
|
17.9
|
1.0
|
OE1
|
B:GLU286
|
4.4
|
15.5
|
1.0
|
N
|
B:SER351
|
4.5
|
15.3
|
1.0
|
CD
|
B:GLU286
|
4.5
|
16.1
|
1.0
|
O
|
B:PHE349
|
4.5
|
18.1
|
1.0
|
C2
|
B:EDO504
|
4.5
|
23.4
|
1.0
|
C1
|
B:EDO504
|
4.8
|
25.3
|
1.0
|
CG1
|
B:VAL372
|
4.9
|
15.1
|
1.0
|
O
|
B:HOH604
|
4.9
|
18.9
|
1.0
|
|
Zinc binding site 4 out
of 4 in 4msd
Go back to
Zinc Binding Sites List in 4msd
Zinc binding site 4 out
of 4 in the Crystal Structure of Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant
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 Schizosaccharomyces Pombe Amsh-Like Protein SST2 T319I Mutant within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn502
b:19.6
occ:1.00
|
NE2
|
B:HIS356
|
2.0
|
20.1
|
1.0
|
NE2
|
B:HIS404
|
2.0
|
21.4
|
1.0
|
NE2
|
B:HIS406
|
2.0
|
20.0
|
1.0
|
SG
|
B:CYS397
|
2.3
|
21.2
|
1.0
|
CE1
|
B:HIS406
|
2.9
|
21.5
|
1.0
|
CE1
|
B:HIS356
|
3.0
|
20.3
|
1.0
|
CD2
|
B:HIS404
|
3.0
|
19.7
|
1.0
|
CE1
|
B:HIS404
|
3.0
|
22.0
|
1.0
|
CD2
|
B:HIS356
|
3.0
|
19.6
|
1.0
|
CD2
|
B:HIS406
|
3.1
|
23.7
|
1.0
|
CB
|
B:CYS397
|
3.2
|
20.9
|
1.0
|
O
|
B:HOH653
|
3.8
|
26.6
|
1.0
|
ND1
|
B:HIS406
|
4.0
|
23.6
|
1.0
|
ND1
|
B:HIS356
|
4.1
|
18.8
|
1.0
|
ND1
|
B:HIS404
|
4.1
|
21.8
|
1.0
|
CG
|
B:HIS404
|
4.1
|
23.2
|
1.0
|
CG
|
B:HIS406
|
4.1
|
23.7
|
1.0
|
CG
|
B:HIS356
|
4.1
|
20.8
|
1.0
|
OG
|
B:SER352
|
4.4
|
20.2
|
1.0
|
CA
|
B:CYS397
|
4.6
|
22.3
|
1.0
|
CD1
|
B:ILE394
|
4.8
|
18.6
|
1.0
|
C
|
B:CYS397
|
4.8
|
25.4
|
1.0
|
O
|
B:CYS397
|
4.8
|
28.7
|
1.0
|
O
|
B:HOH681
|
4.9
|
34.9
|
1.0
|
NH2
|
A:ARG398
|
4.9
|
31.5
|
1.0
|
CB
|
B:LYS399
|
5.0
|
24.8
|
1.0
|
|
Reference:
R.K.Shrestha,
J.A.Ronau,
C.W.Davies,
R.G.Guenette,
E.R.Strieter,
L.N.Paul,
C.Das.
Insights Into the Mechanism of Deubiquitination By Jamm Deubiquitinases From Cocrystal Structures of the Enzyme with the Substrate and Product. Biochemistry V. 53 3199 2014.
ISSN: ISSN 0006-2960
PubMed: 24787148
DOI: 10.1021/BI5003162
Page generated: Sun Oct 27 02:39:03 2024
|