Zinc in PDB 1ibi: Quail Cysteine and Glycine-Rich Protein, uc(Nmr), 15 Minimized Model Structures
Zinc Binding Sites:
The binding sites of Zinc atom in the Quail Cysteine and Glycine-Rich Protein, uc(Nmr), 15 Minimized Model Structures
(pdb code 1ibi). 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), 15 Minimized Model Structures, PDB code: 1ibi:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 1ibi
Go back to
Zinc Binding Sites List in 1ibi
Zinc binding site 1 out
of 2 in the Quail Cysteine and Glycine-Rich Protein, uc(Nmr), 15 Minimized Model Structures
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), 15 Minimized Model Structures within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn195
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:CYS144
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS123
|
2.3
|
0.0
|
1.0
|
CE1
|
A:HIS141
|
2.9
|
0.0
|
1.0
|
HE1
|
A:HIS141
|
3.0
|
0.0
|
1.0
|
HB2
|
A:HIS141
|
3.1
|
0.0
|
1.0
|
CG
|
A:HIS141
|
3.1
|
0.0
|
1.0
|
HB3
|
A:CYS120
|
3.2
|
0.0
|
1.0
|
H
|
A:CYS123
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS123
|
3.2
|
0.0
|
1.0
|
HB2
|
A:CYS144
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS144
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS120
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS144
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS123
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS120
|
3.6
|
0.0
|
1.0
|
CB
|
A:HIS141
|
3.6
|
0.0
|
1.0
|
HB3
|
A:ARG122
|
3.7
|
0.0
|
1.0
|
H
|
A:HIS141
|
3.8
|
0.0
|
1.0
|
N
|
A:CYS123
|
4.0
|
0.0
|
1.0
|
NE2
|
A:HIS141
|
4.1
|
0.0
|
1.0
|
CD2
|
A:HIS141
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS123
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS123
|
4.3
|
0.0
|
1.0
|
HB3
|
A:HIS141
|
4.4
|
0.0
|
1.0
|
H
|
A:ARG122
|
4.5
|
0.0
|
1.0
|
N
|
A:HIS141
|
4.5
|
0.0
|
1.0
|
HB
|
A:VAL127
|
4.6
|
0.0
|
1.0
|
CA
|
A:HIS141
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS120
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS144
|
4.7
|
0.0
|
1.0
|
H
|
A:GLY124
|
4.7
|
0.0
|
1.0
|
CB
|
A:ARG122
|
4.8
|
0.0
|
1.0
|
HB2
|
A:ASP125
|
4.8
|
0.0
|
1.0
|
H
|
A:CYS144
|
4.9
|
0.0
|
1.0
|
H
|
A:ASP125
|
4.9
|
0.0
|
1.0
|
HE2
|
A:HIS141
|
4.9
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 1ibi
Go back to
Zinc Binding Sites List in 1ibi
Zinc binding site 2 out
of 2 in the Quail Cysteine and Glycine-Rich Protein, uc(Nmr), 15 Minimized Model Structures
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), 15 Minimized Model Structures within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn196
b:0.0
occ:1.00
|
SG
|
A:CYS147
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS168
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS171
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS150
|
2.3
|
0.0
|
1.0
|
H
|
A:CYS168
|
2.6
|
0.0
|
1.0
|
H
|
A:CYS150
|
2.9
|
0.0
|
1.0
|
HB2
|
A:CYS168
|
3.1
|
0.0
|
1.0
|
HB3
|
A:CYS171
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS147
|
3.2
|
0.0
|
1.0
|
CB
|
A:CYS168
|
3.2
|
0.0
|
1.0
|
HB2
|
A:CYS147
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS171
|
3.3
|
0.0
|
1.0
|
HB3
|
A:CYS147
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS150
|
3.5
|
0.0
|
1.0
|
HB3
|
A:CYS150
|
3.5
|
0.0
|
1.0
|
N
|
A:CYS168
|
3.5
|
0.0
|
1.0
|
HB3
|
A:LYS149
|
3.5
|
0.0
|
1.0
|
H
|
A:GLY151
|
3.7
|
0.0
|
1.0
|
HB2
|
A:CYS171
|
3.8
|
0.0
|
1.0
|
N
|
A:CYS150
|
3.8
|
0.0
|
1.0
|
H
|
A:LYS152
|
3.9
|
0.0
|
1.0
|
HB3
|
A:LYS152
|
3.9
|
0.0
|
1.0
|
CA
|
A:CYS168
|
3.9
|
0.0
|
1.0
|
CA
|
A:CYS150
|
4.1
|
0.0
|
1.0
|
HB3
|
A:CYS168
|
4.2
|
0.0
|
1.0
|
HB2
|
A:CYS150
|
4.4
|
0.0
|
1.0
|
HA
|
A:TYR167
|
4.4
|
0.0
|
1.0
|
H
|
A:LYS149
|
4.4
|
0.0
|
1.0
|
N
|
A:GLY151
|
4.4
|
0.0
|
1.0
|
H
|
A:CYS171
|
4.4
|
0.0
|
1.0
|
HD13
|
A:LEU154
|
4.5
|
0.0
|
1.0
|
CB
|
A:LYS149
|
4.6
|
0.0
|
1.0
|
HA
|
A:CYS168
|
4.6
|
0.0
|
1.0
|
C
|
A:CYS150
|
4.7
|
0.0
|
1.0
|
C
|
A:TYR167
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS147
|
4.7
|
0.0
|
1.0
|
CA
|
A:CYS171
|
4.7
|
0.0
|
1.0
|
HB2
|
A:LYS152
|
4.8
|
0.0
|
1.0
|
N
|
A:LYS152
|
4.8
|
0.0
|
1.0
|
CB
|
A:LYS152
|
4.8
|
0.0
|
1.0
|
HD21
|
A:LEU154
|
4.9
|
0.0
|
1.0
|
C
|
A:LYS149
|
4.9
|
0.0
|
1.0
|
C
|
A:CYS168
|
5.0
|
0.0
|
1.0
|
|
Reference:
W.Schuler,
K.Kloiber,
T.Matt,
K.Bister,
R.Konrat.
Application of Cross-Correlated uc(Nmr) Spin Relaxation to the Zinc-Finger Protein CRP2(LIM2): Evidence For Collective Motions in Lim Domains. Biochemistry V. 40 9596 2001.
ISSN: ISSN 0006-2960
PubMed: 11583159
DOI: 10.1021/BI010509M
Page generated: Sun Oct 13 03:03:20 2024
|