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Zinc in PDB 1y79: Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp in Complex with A Peptidic Inhibitor

Enzymatic activity of Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp in Complex with A Peptidic Inhibitor

All present enzymatic activity of Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp in Complex with A Peptidic Inhibitor:
3.4.15.5;

Protein crystallography data

The structure of Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp in Complex with A Peptidic Inhibitor, PDB code: 1y79 was solved by M.Comellas-Bigler, R.Lang, W.Bode, K.Maskos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.408, 67.921, 153.591, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 27.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp in Complex with A Peptidic Inhibitor (pdb code 1y79). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp in Complex with A Peptidic Inhibitor, PDB code: 1y79:

Zinc binding site 1 out of 1 in 1y79

Go back to Zinc Binding Sites List in 1y79
Zinc binding site 1 out of 1 in the Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp in Complex with A Peptidic Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp in Complex with A Peptidic Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
1:Zn700

b:24.5
occ:1.00
 NE2 1:HIS469 2.0 18.8 1.0
O 1:TRP702 2.1 26.2 1.0
OE1 1:GLU498 2.1 19.8 1.0
NE2 1:HIS473 2.1 23.1 1.0
C 1:TRP702 2.7 31.3 1.0
CD 1:GLU498 2.8 21.2 1.0
OE2 1:GLU498 2.8 21.1 1.0
OXT 1:TRP702 2.8 29.1 1.0
CE1 1:HIS469 2.9 21.2 1.0
CE1 1:HIS473 3.0 25.0 1.0
CD2 1:HIS469 3.1 19.9 1.0
CD2 1:HIS473 3.2 25.2 1.0
OG 1:SER501 3.6 20.4 1.0
CB 1:SER501 3.9 22.6 1.0
CE2 1:TYR614 3.9 21.4 1.0
ND1 1:HIS469 4.0 19.3 1.0
CA 1:TRP702 4.0 33.0 1.0
ND1 1:HIS473 4.2 23.1 1.0
CG 1:HIS469 4.2 20.5 1.0
CG 1:GLU498 4.3 21.4 1.0
N 1:TRP702 4.3 36.0 1.0
OH 1:TYR614 4.3 23.5 1.0
CG 1:HIS473 4.3 24.8 1.0
CA 1:GLY703 4.3 41.8 1.0
CZ 1:TYR614 4.6 22.4 1.0
OH 1:TYR607 4.6 30.9 1.0
C 1:LYS701 4.8 37.2 1.0
CB 1:TRP702 4.9 34.5 1.0
CB 1:GLU498 4.9 20.2 1.0
OE1 1:GLU470 4.9 24.9 1.0
CA 1:GLU498 4.9 19.7 1.0
CD2 1:TYR614 4.9 22.3 1.0
N 1:LYS701 5.0 40.3 1.0

Reference:

M.Comellas-Bigler, R.Lang, W.Bode, K.Maskos. Crystal Structure of the E.Coli Dipeptidyl Carboxypeptidase Dcp: Further Indication of A Ligand-Dependant Hinge Movement Mechanism J.Mol.Biol. V. 349 99 2005.
ISSN: ISSN 0022-2836
PubMed: 15876371
DOI: 10.1016/J.JMB.2005.03.016
Page generated: Wed Oct 16 20:46:37 2024

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