Zinc in PDB 4ppe: Human RNF4 Ring Domain
Protein crystallography data
The structure of Human RNF4 Ring Domain, PDB code: 4ppe
was solved by
J.J.Perry,
A.S.Arvai,
C.Hitomi,
J.A.Tainer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
28.34 /
2.00
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.938,
86.987,
22.869,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
23 /
28
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Human RNF4 Ring Domain
(pdb code 4ppe). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Human RNF4 Ring Domain, PDB code: 4ppe:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 4ppe
Go back to
Zinc Binding Sites List in 4ppe
Zinc binding site 1 out
of 4 in the Human RNF4 Ring Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Human RNF4 Ring Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn201
b:19.5
occ:1.00
|
SG
|
A:CYS163
|
2.3
|
15.7
|
1.0
|
SG
|
A:CYS136
|
2.4
|
13.3
|
1.0
|
SG
|
A:CYS139
|
2.4
|
21.5
|
1.0
|
SG
|
A:CYS166
|
2.4
|
18.1
|
1.0
|
CB
|
A:CYS136
|
3.0
|
15.9
|
1.0
|
CB
|
A:CYS166
|
3.0
|
12.7
|
1.0
|
CB
|
A:CYS139
|
3.2
|
16.7
|
1.0
|
CB
|
A:CYS163
|
3.4
|
13.3
|
1.0
|
N
|
A:CYS139
|
3.7
|
18.1
|
1.0
|
NH2
|
A:ARG151
|
3.7
|
19.5
|
1.0
|
CA
|
A:CYS139
|
4.1
|
18.4
|
1.0
|
N
|
A:CYS163
|
4.1
|
13.6
|
1.0
|
N
|
A:CYS166
|
4.2
|
16.5
|
1.0
|
CA
|
A:CYS166
|
4.2
|
16.4
|
1.0
|
CA
|
A:CYS163
|
4.3
|
14.0
|
1.0
|
O
|
A:HOH311
|
4.3
|
26.5
|
1.0
|
CA
|
A:CYS136
|
4.5
|
16.1
|
1.0
|
CB
|
A:ILE138
|
4.6
|
14.4
|
1.0
|
O
|
A:CYS163
|
4.7
|
12.3
|
1.0
|
C
|
A:ILE138
|
4.8
|
18.7
|
1.0
|
C
|
A:CYS163
|
4.8
|
12.9
|
1.0
|
CZ
|
A:ARG151
|
4.8
|
18.7
|
1.0
|
C
|
A:CYS139
|
4.9
|
20.9
|
1.0
|
C
|
A:CYS136
|
5.0
|
16.2
|
1.0
|
|
Zinc binding site 2 out
of 4 in 4ppe
Go back to
Zinc Binding Sites List in 4ppe
Zinc binding site 2 out
of 4 in the Human RNF4 Ring Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Human RNF4 Ring Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn202
b:15.2
occ:1.00
|
ND1
|
A:HIS160
|
2.2
|
14.9
|
1.0
|
SG
|
A:CYS158
|
2.4
|
14.2
|
1.0
|
SG
|
A:CYS177
|
2.4
|
19.1
|
1.0
|
SG
|
A:CYS180
|
2.5
|
16.6
|
1.0
|
CE1
|
A:HIS160
|
3.0
|
18.8
|
1.0
|
CB
|
A:CYS177
|
3.1
|
16.2
|
1.0
|
CG
|
A:HIS160
|
3.3
|
16.6
|
1.0
|
CB
|
A:CYS158
|
3.3
|
14.8
|
1.0
|
CB
|
A:CYS180
|
3.5
|
14.4
|
1.0
|
OG1
|
A:THR156
|
3.6
|
19.1
|
1.0
|
CB
|
A:HIS160
|
3.8
|
15.0
|
1.0
|
N
|
A:CYS180
|
3.9
|
15.1
|
1.0
|
NE2
|
A:HIS160
|
4.2
|
18.1
|
1.0
|
CA
|
A:CYS180
|
4.2
|
14.2
|
1.0
|
CD2
|
A:HIS160
|
4.4
|
15.0
|
1.0
|
CA
|
A:CYS158
|
4.5
|
18.8
|
1.0
|
CA
|
A:CYS177
|
4.6
|
17.0
|
1.0
|
CB
|
A:THR179
|
4.6
|
16.2
|
1.0
|
CB
|
A:THR156
|
4.6
|
14.9
|
1.0
|
C
|
A:CYS158
|
4.6
|
16.9
|
1.0
|
N
|
A:HIS160
|
4.8
|
16.0
|
1.0
|
O
|
A:CYS158
|
4.8
|
15.2
|
1.0
|
C
|
A:THR179
|
4.9
|
13.0
|
1.0
|
CG2
|
A:THR156
|
4.9
|
15.0
|
1.0
|
C
|
A:CYS180
|
4.9
|
21.5
|
1.0
|
CA
|
A:HIS160
|
4.9
|
13.0
|
1.0
|
N
|
A:ARG181
|
4.9
|
21.1
|
1.0
|
N
|
A:CYS158
|
5.0
|
15.1
|
1.0
|
CG2
|
A:THR179
|
5.0
|
16.6
|
1.0
|
|
Zinc binding site 3 out
of 4 in 4ppe
Go back to
Zinc Binding Sites List in 4ppe
Zinc binding site 3 out
of 4 in the Human RNF4 Ring Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Human RNF4 Ring Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn201
b:25.1
occ:1.00
|
SG
|
B:CYS136
|
2.4
|
20.2
|
1.0
|
SG
|
B:CYS163
|
2.5
|
20.4
|
1.0
|
SG
|
B:CYS139
|
2.5
|
19.9
|
1.0
|
SG
|
B:CYS166
|
2.5
|
32.5
|
1.0
|
CB
|
B:CYS136
|
3.0
|
17.1
|
1.0
|
CB
|
B:CYS166
|
3.1
|
24.1
|
1.0
|
CB
|
B:CYS139
|
3.2
|
19.5
|
1.0
|
CB
|
B:CYS163
|
3.5
|
18.3
|
1.0
|
N
|
B:CYS139
|
3.6
|
23.8
|
1.0
|
NH2
|
B:ARG151
|
3.9
|
20.8
|
1.0
|
CA
|
B:CYS139
|
4.0
|
21.7
|
1.0
|
N
|
B:CYS163
|
4.0
|
18.2
|
1.0
|
CA
|
B:CYS163
|
4.3
|
20.2
|
1.0
|
N
|
B:CYS166
|
4.3
|
27.9
|
1.0
|
CA
|
B:CYS166
|
4.3
|
24.1
|
1.0
|
CA
|
B:CYS136
|
4.5
|
17.4
|
1.0
|
CB
|
B:ILE138
|
4.6
|
19.8
|
1.0
|
O
|
B:CYS163
|
4.7
|
18.3
|
1.0
|
C
|
B:ILE138
|
4.7
|
20.6
|
1.0
|
C
|
B:CYS163
|
4.8
|
18.6
|
1.0
|
C
|
B:CYS139
|
4.9
|
21.7
|
1.0
|
N
|
B:ILE138
|
4.9
|
19.6
|
1.0
|
CZ
|
B:ARG151
|
4.9
|
23.3
|
1.0
|
N
|
B:MET140
|
4.9
|
19.3
|
1.0
|
C
|
B:CYS136
|
5.0
|
18.5
|
1.0
|
CA
|
B:ILE138
|
5.0
|
17.9
|
1.0
|
|
Zinc binding site 4 out
of 4 in 4ppe
Go back to
Zinc Binding Sites List in 4ppe
Zinc binding site 4 out
of 4 in the Human RNF4 Ring Domain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Human RNF4 Ring Domain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn202
b:22.8
occ:1.00
|
ND1
|
B:HIS160
|
2.1
|
14.5
|
1.0
|
SG
|
B:CYS177
|
2.4
|
21.2
|
1.0
|
SG
|
B:CYS180
|
2.4
|
25.3
|
1.0
|
SG
|
B:CYS158
|
2.4
|
20.3
|
1.0
|
CE1
|
B:HIS160
|
2.9
|
17.0
|
1.0
|
CB
|
B:CYS177
|
3.1
|
17.1
|
1.0
|
CG
|
B:HIS160
|
3.2
|
13.8
|
1.0
|
CB
|
B:CYS180
|
3.4
|
23.4
|
1.0
|
CB
|
B:CYS158
|
3.4
|
20.4
|
1.0
|
CB
|
B:HIS160
|
3.7
|
16.7
|
1.0
|
OG1
|
B:THR156
|
3.8
|
18.8
|
1.0
|
N
|
B:CYS180
|
3.8
|
27.0
|
1.0
|
NE2
|
B:HIS160
|
4.1
|
16.3
|
1.0
|
CA
|
B:CYS180
|
4.2
|
22.6
|
1.0
|
CD2
|
B:HIS160
|
4.3
|
12.8
|
1.0
|
O
|
B:CYS158
|
4.4
|
22.0
|
1.0
|
C
|
B:CYS158
|
4.5
|
18.9
|
1.0
|
CA
|
B:CYS158
|
4.5
|
22.6
|
1.0
|
CA
|
B:CYS177
|
4.6
|
25.9
|
1.0
|
CB
|
B:THR179
|
4.7
|
21.4
|
1.0
|
N
|
B:HIS160
|
4.7
|
14.2
|
1.0
|
CB
|
B:THR156
|
4.7
|
16.8
|
1.0
|
C
|
B:CYS180
|
4.9
|
22.9
|
1.0
|
CA
|
B:HIS160
|
4.9
|
16.5
|
1.0
|
C
|
B:THR179
|
4.9
|
24.1
|
1.0
|
N
|
B:ARG181
|
4.9
|
26.6
|
1.0
|
|
Reference:
L.M.Groocock,
J.Prudden,
Minghua N.,
D.Moiani,
T.Wang,
A.Cheltsov,
R.P.Rambo,
A.S.Arvai,
C.Hitomi,
J.A.Tainer,
J.J.P.Perry,
E.Lazzerini-Denchi,
M.N.Boddy.
RNF4 Requires Both Its Sumo and Nucleosome Interacting Abilities to Promote the Dna Damage Response To Be Published.
Page generated: Sun Oct 27 06:02:30 2024
|