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Zinc in PDB 1exk: Solution Structure of the Cysteine-Rich Domain of the Escherichia Coli Chaperone Protein Dnaj.

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of the Cysteine-Rich Domain of the Escherichia Coli Chaperone Protein Dnaj. (pdb code 1exk). 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 Domain of the Escherichia Coli Chaperone Protein Dnaj., PDB code: 1exk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1exk

Go back to Zinc Binding Sites List in 1exk
Zinc binding site 1 out of 2 in the Solution Structure of the Cysteine-Rich Domain of the Escherichia Coli Chaperone Protein Dnaj.


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 Domain of the Escherichia Coli Chaperone Protein Dnaj. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn80

b:10.0
occ:1.00
SG A:CYS70 2.3 10.0 1.0
SG A:CYS14 2.3 10.0 1.0
SG A:CYS17 2.3 10.0 1.0
SG A:CYS67 2.3 10.0 1.0
HB3 A:CYS14 2.7 10.0 1.0
HB3 A:CYS67 2.7 10.0 1.0
CB A:CYS14 3.0 10.0 1.0
HB3 A:CYS17 3.0 10.0 1.0
CB A:CYS67 3.0 10.0 1.0
CB A:CYS17 3.2 10.0 1.0
HB3 A:CYS70 3.4 10.0 1.0
H A:CYS17 3.4 10.0 1.0
HB2 A:CYS14 3.4 10.0 1.0
HB2 A:CYS67 3.4 10.0 1.0
CB A:CYS70 3.5 10.0 1.0
HA2 A:GLY74 3.5 10.0 1.0
H A:CYS70 3.6 10.0 1.0
HB3 A:LYS69 3.6 10.0 1.0
HA2 A:GLY21 3.9 10.0 1.0
N A:CYS17 3.9 10.0 1.0
HB A:VAL16 4.1 10.0 1.0
HB2 A:CYS17 4.1 10.0 1.0
N A:CYS70 4.1 10.0 1.0
O A:CYS14 4.1 10.0 1.0
O A:CYS67 4.2 10.0 1.0
CA A:CYS17 4.2 10.0 1.0
HG13 A:VAL16 4.2 10.0 1.0
HB2 A:CYS70 4.3 10.0 1.0
CA A:CYS14 4.3 10.0 1.0
CA A:CYS67 4.4 10.0 1.0
CA A:CYS70 4.4 10.0 1.0
CA A:GLY74 4.5 10.0 1.0
H A:GLY74 4.5 10.0 1.0
HD3 A:LYS69 4.6 10.0 1.0
C A:CYS14 4.6 10.0 1.0
C A:CYS67 4.6 10.0 1.0
CB A:LYS69 4.7 10.0 1.0
CA A:GLY21 4.8 10.0 1.0
O A:GLY21 4.8 10.0 1.0
C A:GLY74 4.8 10.0 1.0
HA A:CYS14 4.9 10.0 1.0
N A:GLY74 4.9 10.0 1.0
O A:GLY74 4.9 10.0 1.0
HG2 A:LYS69 4.9 10.0 1.0
CB A:VAL16 4.9 10.0 1.0
C A:VAL16 4.9 10.0 1.0
HA A:CYS17 4.9 10.0 1.0
H A:GLY72 4.9 10.0 1.0
C A:GLY21 4.9 10.0 1.0
C A:LYS69 5.0 10.0 1.0
HA A:CYS67 5.0 10.0 1.0

Zinc binding site 2 out of 2 in 1exk

Go back to Zinc Binding Sites List in 1exk
Zinc binding site 2 out of 2 in the Solution Structure of the Cysteine-Rich Domain of the Escherichia Coli Chaperone Protein Dnaj.


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 Domain of the Escherichia Coli Chaperone Protein Dnaj. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn81

b:10.0
occ:1.00
SG A:CYS56 2.3 10.0 1.0
SG A:CYS31 2.3 10.0 1.0
SG A:CYS53 2.3 10.0 1.0
SG A:CYS34 2.3 10.0 1.0
HB3 A:CYS53 2.7 10.0 1.0
HB3 A:CYS31 2.7 10.0 1.0
CB A:CYS53 2.9 10.0 1.0
CB A:CYS31 3.0 10.0 1.0
HB2 A:CYS53 3.2 10.0 1.0
HB2 A:CYS31 3.2 10.0 1.0
HB A:THR33 3.4 10.0 1.0
HA2 A:GLY60 3.5 10.0 1.0
H A:CYS34 3.6 10.0 1.0
H A:CYS56 3.6 10.0 1.0
HB3 A:CYS56 3.7 10.0 1.0
CB A:CYS56 3.7 10.0 1.0
HB3 A:HIS55 3.7 10.0 1.0
CB A:CYS34 3.7 10.0 1.0
HB3 A:CYS34 3.8 10.0 1.0
HA2 A:GLY38 4.0 10.0 1.0
N A:CYS34 4.1 10.0 1.0
N A:CYS56 4.2 10.0 1.0
CA A:CYS53 4.4 10.0 1.0
H A:GLY60 4.4 10.0 1.0
CA A:CYS31 4.4 10.0 1.0
CB A:THR33 4.4 10.0 1.0
HB2 A:CYS56 4.4 10.0 1.0
CA A:GLY60 4.5 10.0 1.0
HB2 A:CYS34 4.5 10.0 1.0
CA A:CYS34 4.6 10.0 1.0
CA A:CYS56 4.6 10.0 1.0
HG11 A:VAL40 4.6 10.0 1.0
H A:GLY38 4.7 10.0 1.0
OG1 A:THR33 4.7 10.0 1.0
HD21 A:LEU62 4.7 10.0 1.0
O A:CYS31 4.7 10.0 1.0
HG1 A:THR33 4.7 10.0 1.0
C A:CYS31 4.8 10.0 1.0
O A:CYS53 4.8 10.0 1.0
CB A:HIS55 4.8 10.0 1.0
C A:CYS53 4.8 10.0 1.0
HA A:CYS53 4.8 10.0 1.0
HA A:CYS31 4.9 10.0 1.0
CA A:GLY38 4.9 10.0 1.0
N A:GLY60 4.9 10.0 1.0
C A:THR33 4.9 10.0 1.0
C A:GLY60 5.0 10.0 1.0
H A:THR33 5.0 10.0 1.0

Reference:

M.Martinez-Yamout, G.B.Legge, O.Zhang, P.E.Wright, H.J.Dyson. Solution Structure of the Cysteine-Rich Domain of the Escherichia Coli Chaperone Protein Dnaj. J.Mol.Biol. V. 300 805 2000.
ISSN: ISSN 0022-2836
PubMed: 10891270
DOI: 10.1006/JMBI.2000.3923
Page generated: Sun Oct 13 00:33:49 2024

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