Zinc in PDB 1kbf: Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras
Zinc Binding Sites:
The binding sites of Zinc atom in the Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras
(pdb code 1kbf). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras, PDB code: 1kbf:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 1kbf
Go back to
Zinc Binding Sites List in 1kbf
Zinc binding site 1 out
of 2 in the Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1
b:0.0
occ:1.00
|
ND1
|
A:HIS334
|
2.0
|
0.0
|
1.0
|
SG
|
A:CYS377
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS359
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS362
|
2.3
|
0.0
|
1.0
|
O
|
A:LYS360
|
2.4
|
0.0
|
1.0
|
CE1
|
A:HIS334
|
3.0
|
0.0
|
1.0
|
CG
|
A:HIS334
|
3.0
|
0.0
|
1.0
|
HB3
|
A:CYS377
|
3.1
|
0.0
|
1.0
|
H
|
A:CYS362
|
3.1
|
0.0
|
1.0
|
HB2
|
A:HIS361
|
3.1
|
0.0
|
1.0
|
HE1
|
A:HIS334
|
3.2
|
0.0
|
1.0
|
HB3
|
A:HIS334
|
3.3
|
0.0
|
1.0
|
HB2
|
A:CYS359
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS377
|
3.3
|
0.0
|
1.0
|
HB2
|
A:HIS334
|
3.4
|
0.0
|
1.0
|
HB2
|
A:CYS362
|
3.4
|
0.0
|
1.0
|
CB
|
A:HIS334
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS359
|
3.5
|
0.0
|
1.0
|
CB
|
A:CYS362
|
3.5
|
0.0
|
1.0
|
C
|
A:LYS360
|
3.6
|
0.0
|
1.0
|
N
|
A:CYS362
|
3.7
|
0.0
|
1.0
|
H
|
A:ARG363
|
3.9
|
0.0
|
1.0
|
C
|
A:CYS359
|
4.0
|
0.0
|
1.0
|
HB2
|
A:CYS377
|
4.0
|
0.0
|
1.0
|
NE2
|
A:HIS334
|
4.1
|
0.0
|
1.0
|
N
|
A:LYS360
|
4.1
|
0.0
|
1.0
|
CD2
|
A:HIS334
|
4.1
|
0.0
|
1.0
|
CB
|
A:HIS361
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS362
|
4.2
|
0.0
|
1.0
|
O
|
A:CYS359
|
4.2
|
0.0
|
1.0
|
CA
|
A:CYS359
|
4.3
|
0.0
|
1.0
|
HB3
|
A:CYS359
|
4.3
|
0.0
|
1.0
|
H
|
A:LYS360
|
4.3
|
0.0
|
1.0
|
HD2
|
A:HIS361
|
4.3
|
0.0
|
1.0
|
HB3
|
A:CYS362
|
4.4
|
0.0
|
1.0
|
C
|
A:HIS361
|
4.5
|
0.0
|
1.0
|
CA
|
A:CYS377
|
4.5
|
0.0
|
1.0
|
HA
|
A:CYS377
|
4.5
|
0.0
|
1.0
|
CA
|
A:LYS360
|
4.5
|
0.0
|
1.0
|
N
|
A:HIS361
|
4.6
|
0.0
|
1.0
|
O
|
A:ARG378
|
4.6
|
0.0
|
1.0
|
HA
|
A:CYS359
|
4.6
|
0.0
|
1.0
|
CA
|
A:HIS361
|
4.6
|
0.0
|
1.0
|
N
|
A:ARG363
|
4.7
|
0.0
|
1.0
|
HB3
|
A:HIS361
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS377
|
4.8
|
0.0
|
1.0
|
HE2
|
A:HIS334
|
4.9
|
0.0
|
1.0
|
CG
|
A:HIS361
|
4.9
|
0.0
|
1.0
|
C
|
A:CYS362
|
4.9
|
0.0
|
1.0
|
CD2
|
A:HIS361
|
5.0
|
0.0
|
1.0
|
CA
|
A:HIS334
|
5.0
|
0.0
|
1.0
|
O
|
A:CYS377
|
5.0
|
0.0
|
1.0
|
|
Zinc binding site 2 out
of 2 in 1kbf
Go back to
Zinc Binding Sites List in 1kbf
Zinc binding site 2 out
of 2 in the Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Solution Structure of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn2
b:0.0
occ:1.00
|
ND1
|
A:HIS367
|
2.0
|
0.0
|
1.0
|
SG
|
A:CYS349
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS346
|
2.3
|
0.0
|
1.0
|
SG
|
A:CYS370
|
2.3
|
0.0
|
1.0
|
H
|
A:CYS349
|
2.5
|
0.0
|
1.0
|
HB2
|
A:HIS367
|
2.6
|
0.0
|
1.0
|
HB
|
A:VAL348
|
2.8
|
0.0
|
1.0
|
CG
|
A:HIS367
|
2.9
|
0.0
|
1.0
|
CE1
|
A:HIS367
|
3.0
|
0.0
|
1.0
|
CB
|
A:HIS367
|
3.2
|
0.0
|
1.0
|
HB3
|
A:CYS349
|
3.3
|
0.0
|
1.0
|
HE1
|
A:HIS367
|
3.3
|
0.0
|
1.0
|
CB
|
A:CYS349
|
3.3
|
0.0
|
1.0
|
N
|
A:CYS349
|
3.4
|
0.0
|
1.0
|
CB
|
A:CYS346
|
3.4
|
0.0
|
1.0
|
HB3
|
A:CYS346
|
3.5
|
0.0
|
1.0
|
CB
|
A:CYS370
|
3.5
|
0.0
|
1.0
|
HB2
|
A:CYS370
|
3.6
|
0.0
|
1.0
|
HB2
|
A:CYS346
|
3.6
|
0.0
|
1.0
|
HB3
|
A:CYS370
|
3.6
|
0.0
|
1.0
|
HB3
|
A:HIS367
|
3.8
|
0.0
|
1.0
|
CB
|
A:VAL348
|
3.9
|
0.0
|
1.0
|
H
|
A:HIS367
|
3.9
|
0.0
|
1.0
|
CA
|
A:CYS349
|
3.9
|
0.0
|
1.0
|
H
|
A:GLN350
|
4.0
|
0.0
|
1.0
|
CD2
|
A:HIS367
|
4.1
|
0.0
|
1.0
|
NE2
|
A:HIS367
|
4.1
|
0.0
|
1.0
|
H
|
A:VAL348
|
4.1
|
0.0
|
1.0
|
HG21
|
A:VAL348
|
4.3
|
0.0
|
1.0
|
HB2
|
A:CYS349
|
4.3
|
0.0
|
1.0
|
CA
|
A:HIS367
|
4.4
|
0.0
|
1.0
|
HG23
|
A:VAL348
|
4.4
|
0.0
|
1.0
|
C
|
A:VAL348
|
4.4
|
0.0
|
1.0
|
CG2
|
A:VAL348
|
4.4
|
0.0
|
1.0
|
N
|
A:HIS367
|
4.5
|
0.0
|
1.0
|
CA
|
A:VAL348
|
4.6
|
0.0
|
1.0
|
N
|
A:GLN350
|
4.6
|
0.0
|
1.0
|
HG12
|
A:VAL348
|
4.7
|
0.0
|
1.0
|
HG11
|
A:VAL348
|
4.7
|
0.0
|
1.0
|
N
|
A:VAL348
|
4.7
|
0.0
|
1.0
|
CG1
|
A:VAL348
|
4.7
|
0.0
|
1.0
|
HA
|
A:HIS367
|
4.7
|
0.0
|
1.0
|
C
|
A:CYS349
|
4.7
|
0.0
|
1.0
|
HB2
|
A:GLU373
|
4.8
|
0.0
|
1.0
|
HA
|
A:CYS349
|
4.8
|
0.0
|
1.0
|
HG3
|
A:GLU373
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS346
|
4.8
|
0.0
|
1.0
|
CA
|
A:CYS370
|
4.9
|
0.0
|
1.0
|
HE2
|
A:HIS367
|
4.9
|
0.0
|
1.0
|
|
Reference:
M.Zhou,
D.A.Horita,
D.S.Waugh,
R.A.Byrd,
D.K.Morrison.
Solution Structure and Functional Analysis of the Cysteine-Rich C1 Domain of Kinase Suppressor of Ras (Ksr). J.Mol.Biol. V. 315 435 2002.
ISSN: ISSN 0022-2836
PubMed: 11786023
DOI: 10.1006/JMBI.2001.5263
Page generated: Sun Oct 13 04:17:14 2024
|