Zinc in PDB 5d0i: Structure of Ring Finger Protein 165
Protein crystallography data
The structure of Structure of Ring Finger Protein 165, PDB code: 5d0i
was solved by
J.D.Wright,
C.L.Day,
P.D.Mace,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
32.37 /
1.90
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
76.220,
76.220,
103.260,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.3 /
20
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Ring Finger Protein 165
(pdb code 5d0i). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Structure of Ring Finger Protein 165, PDB code: 5d0i:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 5d0i
Go back to
Zinc Binding Sites List in 5d0i
Zinc binding site 1 out
of 4 in the Structure of Ring Finger Protein 165
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of Ring Finger Protein 165 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn401
b:36.6
occ:0.90
|
ND1
|
A:HIS314
|
2.0
|
44.4
|
1.0
|
SG
|
A:CYS331
|
2.3
|
36.7
|
1.0
|
SG
|
A:CYS334
|
2.3
|
41.6
|
1.0
|
SG
|
A:CYS312
|
2.3
|
39.3
|
1.0
|
CE1
|
A:HIS314
|
2.9
|
53.2
|
1.0
|
CB
|
A:CYS331
|
3.0
|
39.2
|
1.0
|
CG
|
A:HIS314
|
3.0
|
38.0
|
1.0
|
CB
|
A:CYS312
|
3.2
|
40.3
|
1.0
|
CB
|
A:HIS314
|
3.5
|
34.9
|
1.0
|
CB
|
A:CYS334
|
3.5
|
40.6
|
1.0
|
N
|
A:CYS334
|
3.8
|
40.0
|
1.0
|
NE2
|
A:HIS314
|
4.1
|
48.6
|
1.0
|
CD2
|
A:HIS314
|
4.1
|
39.5
|
1.0
|
CA
|
A:CYS334
|
4.2
|
40.4
|
1.0
|
CA
|
A:CYS331
|
4.5
|
36.9
|
1.0
|
N
|
A:HIS314
|
4.5
|
36.7
|
1.0
|
CB
|
A:ILE333
|
4.5
|
34.1
|
1.0
|
O
|
A:HOH526
|
4.5
|
44.2
|
1.0
|
CA
|
A:CYS312
|
4.5
|
40.6
|
1.0
|
CA
|
A:HIS314
|
4.6
|
37.2
|
1.0
|
C
|
A:CYS312
|
4.7
|
44.8
|
1.0
|
O
|
A:CYS312
|
4.7
|
46.2
|
1.0
|
C
|
A:ILE333
|
4.8
|
46.2
|
1.0
|
C
|
A:CYS334
|
4.9
|
39.8
|
1.0
|
N
|
A:ILE333
|
5.0
|
32.9
|
1.0
|
|
Zinc binding site 2 out
of 4 in 5d0i
Go back to
Zinc Binding Sites List in 5d0i
Zinc binding site 2 out
of 4 in the Structure of Ring Finger Protein 165
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of Ring Finger Protein 165 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn402
b:28.1
occ:1.00
|
ND1
|
A:HIS317
|
2.1
|
26.3
|
1.0
|
SG
|
A:CYS320
|
2.3
|
27.1
|
1.0
|
SG
|
A:CYS297
|
2.3
|
28.7
|
1.0
|
SG
|
A:CYS294
|
2.4
|
28.3
|
1.0
|
CB
|
A:CYS294
|
3.0
|
27.3
|
1.0
|
CE1
|
A:HIS317
|
3.0
|
30.3
|
1.0
|
CG
|
A:HIS317
|
3.1
|
25.0
|
1.0
|
CB
|
A:CYS297
|
3.2
|
28.2
|
1.0
|
CB
|
A:CYS320
|
3.3
|
27.6
|
1.0
|
CB
|
A:HIS317
|
3.4
|
26.7
|
1.0
|
N
|
A:CYS297
|
3.8
|
28.2
|
1.0
|
CA
|
A:CYS297
|
4.1
|
22.9
|
1.0
|
NE2
|
A:HIS317
|
4.2
|
36.1
|
1.0
|
CD2
|
A:HIS317
|
4.2
|
28.3
|
1.0
|
N
|
A:HIS317
|
4.2
|
31.4
|
1.0
|
CA
|
A:HIS317
|
4.4
|
28.3
|
1.0
|
CA
|
A:CYS294
|
4.5
|
28.1
|
1.0
|
O
|
A:HOH536
|
4.6
|
22.3
|
0.6
|
OG
|
A:SER299
|
4.7
|
54.6
|
1.0
|
CA
|
A:CYS320
|
4.7
|
27.1
|
1.0
|
CB
|
A:ILE296
|
4.8
|
25.6
|
1.0
|
C
|
A:ILE296
|
4.9
|
26.2
|
1.0
|
C
|
A:CYS294
|
4.9
|
35.4
|
1.0
|
O
|
A:CYS294
|
4.9
|
30.2
|
1.0
|
C
|
A:CYS297
|
4.9
|
29.2
|
1.0
|
N
|
A:CYS320
|
5.0
|
25.2
|
1.0
|
|
Zinc binding site 3 out
of 4 in 5d0i
Go back to
Zinc Binding Sites List in 5d0i
Zinc binding site 3 out
of 4 in the Structure of Ring Finger Protein 165
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structure of Ring Finger Protein 165 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn401
b:46.3
occ:1.00
|
ND1
|
B:HIS314
|
2.0
|
52.6
|
1.0
|
SG
|
B:CYS312
|
2.2
|
40.6
|
1.0
|
SG
|
B:CYS331
|
2.2
|
40.8
|
1.0
|
SG
|
B:CYS334
|
2.4
|
49.4
|
1.0
|
CE1
|
B:HIS314
|
3.0
|
59.8
|
1.0
|
CB
|
B:CYS331
|
3.0
|
41.8
|
1.0
|
CG
|
B:HIS314
|
3.1
|
50.8
|
1.0
|
CB
|
B:CYS312
|
3.3
|
43.3
|
1.0
|
CB
|
B:CYS334
|
3.4
|
47.0
|
1.0
|
CB
|
B:HIS314
|
3.5
|
44.9
|
1.0
|
N
|
B:CYS334
|
3.8
|
53.2
|
1.0
|
NE2
|
B:HIS314
|
4.1
|
56.9
|
1.0
|
CA
|
B:CYS334
|
4.1
|
56.0
|
1.0
|
CD2
|
B:HIS314
|
4.2
|
54.3
|
1.0
|
CA
|
B:CYS331
|
4.5
|
36.4
|
1.0
|
N
|
B:HIS314
|
4.5
|
45.2
|
1.0
|
CA
|
B:CYS312
|
4.5
|
49.6
|
1.0
|
CB
|
B:ILE333
|
4.6
|
47.7
|
1.0
|
O
|
B:CYS312
|
4.6
|
50.7
|
1.0
|
CA
|
B:HIS314
|
4.6
|
50.3
|
1.0
|
C
|
B:CYS312
|
4.6
|
48.8
|
1.0
|
C
|
B:CYS334
|
4.8
|
54.5
|
1.0
|
C
|
B:ILE333
|
4.8
|
55.4
|
1.0
|
N
|
B:ILE333
|
4.9
|
46.4
|
1.0
|
N
|
B:ARG335
|
5.0
|
52.8
|
1.0
|
|
Zinc binding site 4 out
of 4 in 5d0i
Go back to
Zinc Binding Sites List in 5d0i
Zinc binding site 4 out
of 4 in the Structure of Ring Finger Protein 165
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structure of Ring Finger Protein 165 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn402
b:36.0
occ:1.00
|
ND1
|
B:HIS317
|
2.1
|
37.5
|
1.0
|
SG
|
B:CYS294
|
2.3
|
35.6
|
1.0
|
SG
|
B:CYS320
|
2.3
|
32.0
|
1.0
|
SG
|
B:CYS297
|
2.3
|
40.0
|
1.0
|
CB
|
B:CYS294
|
2.9
|
37.4
|
1.0
|
CE1
|
B:HIS317
|
3.0
|
39.0
|
1.0
|
CG
|
B:HIS317
|
3.1
|
35.9
|
1.0
|
CB
|
B:CYS320
|
3.3
|
29.6
|
1.0
|
CB
|
B:CYS297
|
3.3
|
34.0
|
1.0
|
CB
|
B:HIS317
|
3.4
|
33.9
|
1.0
|
N
|
B:CYS297
|
3.8
|
36.4
|
1.0
|
N
|
B:HIS317
|
4.1
|
33.8
|
1.0
|
O
|
B:HOH524
|
4.1
|
46.1
|
1.0
|
CA
|
B:CYS297
|
4.1
|
33.9
|
1.0
|
NE2
|
B:HIS317
|
4.2
|
40.2
|
1.0
|
CD2
|
B:HIS317
|
4.2
|
37.5
|
1.0
|
CA
|
B:HIS317
|
4.3
|
35.4
|
1.0
|
CA
|
B:CYS294
|
4.3
|
40.2
|
1.0
|
CB
|
B:ILE296
|
4.6
|
31.7
|
1.0
|
O
|
B:HOH526
|
4.7
|
39.8
|
1.0
|
CA
|
B:CYS320
|
4.7
|
26.9
|
1.0
|
O
|
B:CYS294
|
4.8
|
51.0
|
1.0
|
C
|
B:CYS294
|
4.8
|
47.0
|
1.0
|
C
|
B:ILE296
|
4.8
|
46.0
|
1.0
|
C
|
B:CYS297
|
4.9
|
42.8
|
1.0
|
N
|
B:ILE296
|
5.0
|
38.3
|
1.0
|
|
Reference:
J.D.Wright,
P.D.Mace,
C.L.Day.
Secondary Ubiquitin-Ring Docking Enhances Arkadia and ARK2C E3 Ligase Activity. Nat.Struct.Mol.Biol. V. 23 45 2016.
ISSN: ESSN 1545-9985
PubMed: 26656854
DOI: 10.1038/NSMB.3142
Page generated: Sun Oct 27 14:31:47 2024
|