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Zinc in PDB 1hdq: Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with D-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A

Enzymatic activity of Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with D-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A

All present enzymatic activity of Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with D-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A:
3.4.17.1;

Protein crystallography data

The structure of Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with D-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A, PDB code: 1hdq was solved by J.H.Cho, N.-C.Ha, S.J.Chung, D.H.Kim, K.Y.Choi, B.-H.Oh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100 / 2.3
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.961, 60.465, 47.792, 90.00, 97.59, 90.00
R / Rfree (%) 13.88 / 17.44

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with D-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A (pdb code 1hdq). 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 Bovine Pancreatic Carboxypeptidase A Complexed with D-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A, PDB code: 1hdq:

Zinc binding site 1 out of 1 in 1hdq

Go back to Zinc Binding Sites List in 1hdq
Zinc binding site 1 out of 1 in the Crystal Structure of Bovine Pancreatic Carboxypeptidase A Complexed with D-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A


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 Bovine Pancreatic Carboxypeptidase A Complexed with D-N-Hydroxyaminocarbonyl Phenylalanine at 2.3 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1309

b:11.1
occ:1.00
 O2 A:INF1308 2.2 16.2 1.0
ND1 A:HIS69 2.2 7.2 1.0
ND1 A:HIS196 2.3 7.4 1.0
OE2 A:GLU72 2.4 10.0 1.0
OE1 A:GLU72 2.4 10.2 1.0
CD A:GLU72 2.7 9.6 1.0
N2 A:INF1308 3.0 18.5 1.0
CG A:HIS69 3.1 8.3 1.0
CE1 A:HIS69 3.2 8.4 1.0
CG A:HIS196 3.2 8.2 1.0
CE1 A:HIS196 3.3 7.6 1.0
CB A:HIS196 3.4 6.8 1.0
CB A:HIS69 3.4 9.1 1.0
O A:HOH2070 4.1 9.1 1.0
C1 A:INF1308 4.1 19.2 1.0
O A:SER197 4.1 10.9 1.0
CG A:GLU72 4.2 11.2 1.0
O A:HOH2069 4.2 14.8 1.0
NE2 A:HIS69 4.2 12.1 1.0
CD2 A:HIS69 4.3 8.6 1.0
OE2 A:GLU270 4.3 12.5 1.0
CA A:HIS196 4.3 8.4 1.0
CD2 A:HIS196 4.3 9.0 1.0
O A:HOH2209 4.3 44.7 1.0
NE2 A:HIS196 4.4 9.7 1.0
N A:INF1308 4.4 18.6 1.0
N A:SER197 4.5 8.0 1.0
NH2 A:ARG127 4.8 24.5 1.0
CA A:HIS69 4.8 9.4 1.0
OE1 A:GLU270 4.8 9.6 1.0
C A:HIS196 5.0 8.3 1.0
N A:HIS69 5.0 9.5 1.0

Reference:

J.H.Cho, D.H.Kim, S.J.Chung, N.-C.Ha, B.-H.Oh, K.Y.Choi. Insight Into the Stereochemistry in the Inhibition of Carboxypeptidase A with N- (Hydroxyaminocarbonyl)Phenylalanine: Binding Modes of An Enantiomeric Pair of the Inhibitor to Carboxypeptidase A Bioorg.Med.Chem. V. 10 2015 2002.
ISSN: ISSN 0968-0896
PubMed: 11937361
DOI: 10.1016/S0968-0896(01)00429-1
Page generated: Sun Oct 13 02:08:16 2024

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