Zinc in PDB 5c4v: Ski-Like Protein
Protein crystallography data
The structure of Ski-Like Protein, PDB code: 5c4v
was solved by
K.Wallden,
T.Nyman,
B.M.Hallberg,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.30 /
2.60
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
213.540,
122.830,
51.570,
90.00,
90.72,
90.00
|
R / Rfree (%)
|
20.8 /
24.2
|
Other elements in 5c4v:
The structure of Ski-Like Protein also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Ski-Like Protein
(pdb code 5c4v). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Ski-Like Protein, PDB code: 5c4v:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 5c4v
Go back to
Zinc Binding Sites List in 5c4v
Zinc binding site 1 out
of 3 in the Ski-Like Protein
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Ski-Like Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn401
b:48.4
occ:1.00
|
SG
|
B:CYS291
|
1.6
|
31.5
|
1.0
|
NE2
|
B:HIS306
|
1.9
|
15.8
|
1.0
|
SG
|
B:CYS294
|
2.0
|
33.3
|
1.0
|
NE2
|
B:HIS308
|
2.0
|
29.9
|
1.0
|
CE1
|
B:HIS306
|
2.5
|
17.1
|
1.0
|
CE1
|
B:HIS308
|
2.6
|
26.9
|
1.0
|
CB
|
B:CYS294
|
3.0
|
30.6
|
1.0
|
CD2
|
B:HIS308
|
3.1
|
32.0
|
1.0
|
CB
|
B:CYS291
|
3.2
|
37.0
|
1.0
|
CD2
|
B:HIS306
|
3.2
|
16.8
|
1.0
|
ND1
|
B:HIS308
|
3.7
|
27.4
|
1.0
|
ND1
|
B:HIS306
|
3.7
|
18.6
|
1.0
|
N
|
B:CYS294
|
3.8
|
35.8
|
1.0
|
CG
|
B:HIS308
|
3.9
|
30.1
|
1.0
|
CA
|
B:CYS294
|
4.0
|
31.1
|
1.0
|
CG
|
B:HIS306
|
4.1
|
19.1
|
1.0
|
CB
|
B:GLU293
|
4.5
|
33.1
|
1.0
|
CA
|
B:CYS291
|
4.7
|
40.3
|
1.0
|
CZ
|
B:PHE298
|
4.8
|
31.0
|
1.0
|
CE1
|
B:PHE298
|
4.8
|
33.2
|
1.0
|
C
|
B:GLU293
|
4.8
|
44.1
|
1.0
|
NI
|
B:NI402
|
4.8
|
86.9
|
1.0
|
C
|
B:CYS294
|
4.9
|
35.3
|
1.0
|
|
Zinc binding site 2 out
of 3 in 5c4v
Go back to
Zinc Binding Sites List in 5c4v
Zinc binding site 2 out
of 3 in the Ski-Like Protein
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Ski-Like Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn401
b:57.9
occ:1.00
|
NE2
|
D:HIS306
|
2.2
|
46.2
|
1.0
|
SG
|
D:CYS294
|
2.2
|
52.4
|
1.0
|
NE2
|
D:HIS308
|
2.2
|
68.2
|
1.0
|
SG
|
D:CYS291
|
2.3
|
51.3
|
1.0
|
CE1
|
D:HIS308
|
2.6
|
70.9
|
1.0
|
CE1
|
D:HIS306
|
2.9
|
50.2
|
1.0
|
CB
|
D:CYS291
|
3.1
|
64.2
|
1.0
|
CB
|
D:CYS294
|
3.2
|
52.9
|
1.0
|
CD2
|
D:HIS308
|
3.2
|
67.0
|
1.0
|
CD2
|
D:HIS306
|
3.3
|
54.1
|
1.0
|
N
|
D:CYS294
|
3.5
|
56.6
|
1.0
|
ND1
|
D:HIS308
|
3.6
|
69.8
|
1.0
|
CA
|
D:CYS294
|
3.9
|
51.3
|
1.0
|
CG
|
D:HIS308
|
4.0
|
64.8
|
1.0
|
ND1
|
D:HIS306
|
4.1
|
52.0
|
1.0
|
CB
|
D:GLU293
|
4.1
|
59.8
|
1.0
|
CG
|
D:HIS306
|
4.3
|
50.8
|
1.0
|
C
|
D:GLU293
|
4.5
|
56.6
|
1.0
|
CA
|
D:CYS291
|
4.6
|
65.6
|
1.0
|
CA
|
D:GLU293
|
4.7
|
56.5
|
1.0
|
N
|
D:GLU293
|
4.7
|
56.5
|
1.0
|
SG
|
D:CYS272
|
4.7
|
74.4
|
1.0
|
C
|
D:CYS294
|
4.8
|
54.3
|
1.0
|
CE1
|
D:PHE298
|
4.8
|
57.3
|
1.0
|
C
|
D:CYS291
|
4.9
|
58.8
|
1.0
|
CZ
|
D:PHE298
|
4.9
|
52.0
|
1.0
|
|
Zinc binding site 3 out
of 3 in 5c4v
Go back to
Zinc Binding Sites List in 5c4v
Zinc binding site 3 out
of 3 in the Ski-Like Protein
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Ski-Like Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Zn401
b:41.7
occ:1.00
|
NE2
|
F:HIS308
|
1.5
|
36.4
|
1.0
|
CE1
|
F:HIS308
|
1.9
|
39.0
|
1.0
|
NE2
|
F:HIS306
|
1.9
|
27.1
|
1.0
|
SG
|
F:CYS294
|
2.0
|
40.7
|
1.0
|
SG
|
F:CYS291
|
2.2
|
31.0
|
1.0
|
CB
|
F:CYS291
|
2.8
|
30.1
|
1.0
|
CD2
|
F:HIS308
|
2.8
|
39.6
|
1.0
|
CE1
|
F:HIS306
|
2.8
|
27.7
|
1.0
|
CD2
|
F:HIS306
|
3.0
|
25.5
|
1.0
|
ND1
|
F:HIS308
|
3.1
|
35.4
|
1.0
|
CB
|
F:CYS294
|
3.2
|
40.8
|
1.0
|
N
|
F:CYS294
|
3.5
|
44.8
|
1.0
|
CG
|
F:HIS308
|
3.5
|
37.5
|
1.0
|
CA
|
F:CYS294
|
3.9
|
44.5
|
1.0
|
ND1
|
F:HIS306
|
4.0
|
28.5
|
1.0
|
CG
|
F:HIS306
|
4.1
|
28.6
|
1.0
|
CA
|
F:CYS291
|
4.2
|
33.1
|
1.0
|
CE1
|
F:PHE298
|
4.4
|
30.9
|
1.0
|
CB
|
F:GLU293
|
4.5
|
52.6
|
1.0
|
CZ
|
F:PHE298
|
4.6
|
36.7
|
1.0
|
C
|
F:GLU293
|
4.6
|
51.9
|
1.0
|
C
|
F:CYS294
|
4.7
|
45.5
|
1.0
|
C
|
F:CYS291
|
4.7
|
35.2
|
1.0
|
SG
|
F:CYS272
|
4.7
|
35.7
|
1.0
|
O
|
F:CYS291
|
4.8
|
38.6
|
1.0
|
N
|
F:GLU293
|
4.8
|
47.9
|
1.0
|
N
|
F:CYS295
|
4.8
|
46.0
|
1.0
|
CA
|
F:GLU293
|
4.9
|
48.6
|
1.0
|
|
Reference:
K.Wallden,
T.Nyman,
B.M.Hallberg.
Snon Stabilizes the SMAD3/SMAD4 Protein Complex. Sci Rep V. 7 46370 2017.
ISSN: ESSN 2045-2322
PubMed: 28397834
DOI: 10.1038/SREP46370
Page generated: Sun Oct 27 13:51:17 2024
|