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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

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