Zinc in PDB 8cpa: Comparison of the Structures of Three Carboxypeptidase A- Phosphonate Complexes Determined By X-Ray Crystallography

Enzymatic activity of Comparison of the Structures of Three Carboxypeptidase A- Phosphonate Complexes Determined By X-Ray Crystallography

All present enzymatic activity of Comparison of the Structures of Three Carboxypeptidase A- Phosphonate Complexes Determined By X-Ray Crystallography:
3.4.17.1;

Protein crystallography data

The structure of Comparison of the Structures of Three Carboxypeptidase A- Phosphonate Complexes Determined By X-Ray Crystallography, PDB code: 8cpa was solved by H.Kim, W.N.Lipscomb, 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 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.400, 65.900, 74.400, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Comparison of the Structures of Three Carboxypeptidase A- Phosphonate Complexes Determined By X-Ray Crystallography (pdb code 8cpa). 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 Comparison of the Structures of Three Carboxypeptidase A- Phosphonate Complexes Determined By X-Ray Crystallography, PDB code: 8cpa:

Zinc binding site 1 out of 1 in 8cpa

Go back to Zinc Binding Sites List in 8cpa
Zinc binding site 1 out of 1 in the Comparison of the Structures of Three Carboxypeptidase A- Phosphonate Complexes Determined By X-Ray Crystallography


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Comparison of the Structures of Three Carboxypeptidase A- Phosphonate Complexes Determined By X-Ray Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn308

b:8.7
occ:1.00
 O1P A:AGF309 1.9 27.3 1.0
ND1 A:HIS69 2.1 7.7 1.0
ND1 A:HIS196 2.1 9.5 1.0
OE2 A:GLU72 2.2 10.2 1.0
OE1 A:GLU72 2.2 9.9 1.0
CD A:GLU72 2.6 8.9 1.0
CG A:HIS69 2.9 5.3 1.0
P3 A:AGF309 2.9 16.0 1.0
CG A:HIS196 3.1 7.7 1.0
CE1 A:HIS196 3.1 7.8 1.0
O2P A:AGF309 3.2 24.0 1.0
CB A:HIS69 3.3 7.0 1.0
CE1 A:HIS69 3.3 5.1 1.0
CB A:HIS196 3.5 4.5 1.0
O A:HOH310 4.0 2.8 1.0
NH1 A:ARG127 4.1 6.0 1.0
CA3 A:AGF309 4.1 15.5 1.0
CG A:GLU72 4.1 5.7 1.0
O3P A:AGF309 4.1 16.9 1.0
CD2 A:HIS69 4.2 5.4 1.0
O A:HOH317 4.2 8.2 1.0
NE2 A:HIS196 4.2 7.4 1.0
CA4 A:AGF309 4.2 21.1 1.0
CD2 A:HIS196 4.2 7.8 1.0
NE2 A:HIS69 4.3 5.6 1.0
O A:SER197 4.3 6.3 1.0
O42 A:AGF309 4.4 20.9 1.0
C4 A:AGF309 4.4 12.4 1.0
CA A:HIS196 4.5 3.0 1.0
CA A:HIS69 4.7 6.8 1.0
N A:SER197 4.7 6.5 1.0
CZ A:ARG127 4.9 5.0 1.0
N A:HIS69 4.9 8.0 1.0
O2 A:AGF309 5.0 22.9 1.0
N3 A:AGF309 5.0 13.9 1.0

Reference:

H.Kim, W.N.Lipscomb. Comparison of the Structures of Three Carboxypeptidase A-Phosphonate Complexes Determined By X-Ray Crystallography. Biochemistry V. 30 8171 1991.
ISSN: ISSN 0006-2960
PubMed: 1868092
DOI: 10.1021/BI00247A012
Page generated: Wed Dec 16 14:05:12 2020

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