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Zinc in PDB 1cbx: Crystal Structure of the Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 Angstroms Resolution

Enzymatic activity of Crystal Structure of the Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 Angstroms Resolution

All present enzymatic activity of Crystal Structure of the Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 Angstroms Resolution:
3.4.17.1;

Protein crystallography data

The structure of Crystal Structure of the Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 Angstroms Resolution, PDB code: 1cbx was solved by S.Mangani, P.Carloni, P.Orioli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.600, 60.270, 47.250, 90.00, 97.27, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 Angstroms Resolution (pdb code 1cbx). 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 Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 Angstroms Resolution, PDB code: 1cbx:

Zinc binding site 1 out of 1 in 1cbx

Go back to Zinc Binding Sites List in 1cbx
Zinc binding site 1 out of 1 in the Crystal Structure of the Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 Angstroms Resolution


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 Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn309

b:5.6
occ:1.00
 ND1 A:HIS196 2.0 3.0 1.0
OE2 A:GLU72 2.0 3.0 1.0
ND1 A:HIS69 2.0 3.0 1.0
O1 A:BZS500 2.3 13.9 1.0
O2 A:BZS500 2.6 12.2 1.0
CD A:GLU72 2.7 14.8 1.0
C1 A:BZS500 2.7 17.0 1.0
OE1 A:GLU72 2.8 4.5 1.0
CE1 A:HIS196 2.8 10.0 1.0
CG A:HIS69 3.0 3.9 1.0
CE1 A:HIS69 3.1 3.6 1.0
CG A:HIS196 3.2 8.2 1.0
CB A:HIS69 3.3 15.8 1.0
CB A:HIS196 3.7 3.0 1.0
O A:HOH663 3.9 12.4 1.0
NH1 A:ARG127 3.9 16.6 1.0
NE2 A:HIS196 4.0 3.0 1.0
CD2 A:HIS69 4.1 6.8 1.0
NE2 A:HIS69 4.1 10.7 1.0
C2 A:BZS500 4.2 9.6 1.0
O A:SER197 4.2 13.9 1.0
CG A:GLU72 4.2 12.2 1.0
CD2 A:HIS196 4.2 7.3 1.0
O A:HOH660 4.3 22.6 1.0
O3 A:BZS500 4.4 15.7 1.0
CA A:BZS500 4.5 11.2 1.0
C A:BZS500 4.6 19.3 1.0
O A:HOH645 4.6 5.6 1.0
CA A:HIS196 4.6 9.2 1.0
CA A:HIS69 4.7 3.0 1.0
CZ A:ARG127 4.8 14.4 1.0
N A:SER197 4.9 3.0 1.0
OE1 A:GLU270 4.9 3.0 1.0
N A:HIS69 4.9 7.1 1.0
NH2 A:ARG127 5.0 3.0 1.0

Reference:

S.Mangani, P.Carloni, P.Orioli. Crystal Structure of the Complex Between Carboxypeptidase A and the Biproduct Analog Inhibitor L-Benzylsuccinate at 2.0 A Resolution. J.Mol.Biol. V. 223 573 1992.
ISSN: ISSN 0022-2836
PubMed: 1738164
DOI: 10.1016/0022-2836(92)90671-6
Page generated: Sat Oct 12 23:02:17 2024

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