Zinc in PDB 1qli: Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Average Structure
Zinc Binding Sites:
The binding sites of Zinc atom in the Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Average Structure
(pdb code 1qli). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Average Structure, PDB code: 1qli:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 1qli
Go back to
Zinc Binding Sites List in 1qli
Zinc binding site 1 out
of 2 in the Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Average Structure
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Average Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn195
b:0.0
occ:1.00
|
SG
|
A:CYS147
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS171
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS168
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS150
|
2.3
|
0.0
|
1.0
|
H
|
A:CYS150
|
3.0
|
0.0
|
1.0
|
HG3
|
A:LYS149
|
3.0
|
0.0
|
1.0
|
HB3
|
A:CYS168
|
3.1
|
0.0
|
1.0
|
HB2
|
A:CYS147
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS150
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS147
|
3.2
|
0.0
|
1.0
|
HB2
|
A:CYS171
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS168
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS150
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS171
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS147
|
3.4
|
0.0
|
1.0
|
H
|
A:CYS168
|
3.4
|
0.0
|
1.0
|
H
|
A:CYS171
|
3.6
|
0.0
|
1.0
|
HZ3
|
A:LYS174
|
3.8
|
0.0
|
1.0
|
N
|
A:CYS150
|
3.8
|
0.0
|
1.0
|
N
|
A:CYS171
|
3.9
|
0.0
|
1.0
|
HD2
|
A:LYS149
|
3.9
|
0.0
|
1.0
|
CA
|
A:CYS171
|
4.0
|
0.0
|
1.0
|
CG
|
A:LYS149
|
4.0
|
0.0
|
1.0
|
HA
|
A:CYS171
|
4.0
|
0.0
|
1.0
|
HB2
|
A:LYS152
|
4.0
|
0.0
|
1.0
|
HD23
|
A:LEU154
|
4.1
|
0.0
|
1.0
|
CA
|
A:CYS150
|
4.1
|
0.0
|
1.0
|
N
|
A:CYS168
|
4.1
|
0.0
|
1.0
|
HB2
|
A:CYS168
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS168
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS150
|
4.2
|
0.0
|
1.0
|
O
|
A:CYS168
|
4.2
|
0.0
|
1.0
|
HB3
|
A:CYS171
|
4.2
|
0.0
|
1.0
|
H
|
A:LYS152
|
4.3
|
0.0
|
1.0
|
HD3
|
A:LYS149
|
4.3
|
0.0
|
1.0
|
HG2
|
A:LYS149
|
4.3
|
0.0
|
1.0
|
CD
|
A:LYS149
|
4.3
|
0.0
|
1.0
|
HD2
|
A:LYS152
|
4.3
|
0.0
|
1.0
|
H
|
A:LYS149
|
4.4
|
0.0
|
1.0
|
H
|
A:GLY151
|
4.5
|
0.0
|
1.0
|
HZ2
|
A:LYS174
|
4.5
|
0.0
|
1.0
|
C
|
A:CYS168
|
4.5
|
0.0
|
1.0
|
NZ
|
A:LYS174
|
4.6
|
0.0
|
1.0
|
CA
|
A:CYS147
|
4.6
|
0.0
|
1.0
|
HD12
|
A:LEU154
|
4.7
|
0.0
|
1.0
|
C
|
A:GLY170
|
4.8
|
0.0
|
1.0
|
C
|
A:CYS150
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS147
|
4.8
|
0.0
|
1.0
|
N
|
A:GLY151
|
4.9
|
0.0
|
1.0
|
HA3
|
A:GLY170
|
4.9
|
0.0
|
1.0
|
H
|
A:GLY170
|
5.0
|
0.0
|
1.0
|
HG3
|
A:LYS152
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 1qli
Go back to
Zinc Binding Sites List in 1qli
Zinc binding site 2 out
of 2 in the Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Average Structure
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Quail Cysteine and Glycine-Rich Protein, uc(Nmr), Minimized Average Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn196
b:0.0
occ:1.00
|
ND1
|
A:HIS141
|
2.0
|
0.0
|
1.0
|
SG
|
A:CYS120
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS123
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS144
|
2.3
|
0.0
|
1.0
|
HB2
|
A:HIS141
|
2.8
|
0.0
|
1.0
|
H
|
A:CYS123
|
2.8
|
0.0
|
1.0
|
CE1
|
A:HIS141
|
3.0
|
0.0
|
1.0
|
CG
|
A:HIS141
|
3.0
|
0.0
|
1.0
|
HB3
|
A:CYS120
|
3.0
|
0.0
|
1.0
|
HB3
|
A:CYS123
|
3.1
|
0.0
|
1.0
|
HE1
|
A:HIS141
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS120
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS123
|
3.3
|
0.0
|
1.0
|
HB3
|
A:ARG122
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS144
|
3.4
|
0.0
|
1.0
|
CB
|
A:HIS141
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS144
|
3.4
|
0.0
|
1.0
|
HB3
|
A:CYS144
|
3.6
|
0.0
|
1.0
|
HB2
|
A:CYS120
|
3.6
|
0.0
|
1.0
|
N
|
A:CYS123
|
3.7
|
0.0
|
1.0
|
HB3
|
A:HIS141
|
3.9
|
0.0
|
1.0
|
H
|
A:GLY124
|
3.9
|
0.0
|
1.0
|
HE
|
A:ARG122
|
4.0
|
0.0
|
1.0
|
NE2
|
A:HIS141
|
4.1
|
0.0
|
1.0
|
CA
|
A:CYS123
|
4.1
|
0.0
|
1.0
|
HB2
|
A:CYS123
|
4.2
|
0.0
|
1.0
|
CD2
|
A:HIS141
|
4.2
|
0.0
|
1.0
|
H
|
A:ARG122
|
4.2
|
0.0
|
1.0
|
H
|
A:ASP125
|
4.2
|
0.0
|
1.0
|
CB
|
A:ARG122
|
4.3
|
0.0
|
1.0
|
HB2
|
A:ARG122
|
4.4
|
0.0
|
1.0
|
HB2
|
A:ASP125
|
4.4
|
0.0
|
1.0
|
HH21
|
A:ARG122
|
4.4
|
0.0
|
1.0
|
O
|
A:CYS120
|
4.5
|
0.0
|
1.0
|
CA
|
A:CYS120
|
4.6
|
0.0
|
1.0
|
CA
|
A:HIS141
|
4.7
|
0.0
|
1.0
|
N
|
A:HIS141
|
4.7
|
0.0
|
1.0
|
H
|
A:HIS141
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS144
|
4.8
|
0.0
|
1.0
|
N
|
A:GLY124
|
4.8
|
0.0
|
1.0
|
H
|
A:CYS144
|
4.8
|
0.0
|
1.0
|
C
|
A:ARG122
|
4.8
|
0.0
|
1.0
|
C
|
A:CYS120
|
4.8
|
0.0
|
1.0
|
NE
|
A:ARG122
|
4.9
|
0.0
|
1.0
|
HA
|
A:CYS123
|
4.9
|
0.0
|
1.0
|
N
|
A:ARG122
|
4.9
|
0.0
|
1.0
|
CA
|
A:ARG122
|
4.9
|
0.0
|
1.0
|
|
Reference:
R.Konrat,
R.Weiskirchen,
B.Krautler,
K.Bister.
Solution Structure of the Carboxyl-Terminal Lim Domain From Quail Cysteine-Rich Protein CRP2. J.Biol.Chem. V. 272 12001 1997.
ISSN: ISSN 0021-9258
PubMed: 9115265
DOI: 10.1074/JBC.272.18.12001
Page generated: Wed Oct 16 18:12:52 2024
|