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Zinc in PDB 1dtd: Crystal Structure of the Complex Between the Leech Carboxypeptidase Inhibitor and the Human Carboxypeptidase A2 (Lci-CPA2)

Enzymatic activity of Crystal Structure of the Complex Between the Leech Carboxypeptidase Inhibitor and the Human Carboxypeptidase A2 (Lci-CPA2)

All present enzymatic activity of Crystal Structure of the Complex Between the Leech Carboxypeptidase Inhibitor and the Human Carboxypeptidase A2 (Lci-CPA2):
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of the Complex Between the Leech Carboxypeptidase Inhibitor and the Human Carboxypeptidase A2 (Lci-CPA2), PDB code: 1dtd was solved by D.Reverter, C.Fernandez-Catalan, W.Bode, T.A.Holak, F.X.Aviles, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 1.65
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 80.439, 80.439, 114.464, 90.00, 90.00, 120.00
R / Rfree (%) 18.7 / 23.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Complex Between the Leech Carboxypeptidase Inhibitor and the Human Carboxypeptidase A2 (Lci-CPA2) (pdb code 1dtd). 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 the Leech Carboxypeptidase Inhibitor and the Human Carboxypeptidase A2 (Lci-CPA2), PDB code: 1dtd:

Zinc binding site 1 out of 1 in 1dtd

Go back to Zinc Binding Sites List in 1dtd
Zinc binding site 1 out of 1 in the Crystal Structure of the Complex Between the Leech Carboxypeptidase Inhibitor and the Human Carboxypeptidase A2 (Lci-CPA2)


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 the Leech Carboxypeptidase Inhibitor and the Human Carboxypeptidase A2 (Lci-CPA2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:18.5
occ:1.00
 ND1 A:HIS552 2.3 18.2 1.0
ND1 A:HIS424 2.4 17.5 1.0
O B:VAL66 2.5 18.1 1.0
OE2 A:GLU427 2.8 35.7 1.0
OXT B:VAL66 2.8 16.6 1.0
OXT A:GLU300 2.9 40.0 1.0
OE1 A:GLU427 2.9 16.7 1.0
CD A:GLU427 3.0 26.7 1.0
C B:VAL66 3.1 18.9 1.0
CE1 A:HIS552 3.1 17.5 1.0
CG A:HIS424 3.3 17.1 1.0
CG A:HIS552 3.3 17.0 1.0
CE1 A:HIS424 3.3 18.2 1.0
CB A:HIS424 3.5 13.8 1.0
CB A:HIS552 3.6 14.8 1.0
NH2 A:ARG482 4.0 15.5 1.0
O B:HOH67 4.1 19.4 1.0
C A:GLU300 4.1 23.6 1.0
NE2 A:HIS552 4.2 16.5 1.0
CG A:GLU427 4.3 19.2 1.0
O A:HOH2 4.3 17.4 1.0
CA B:VAL66 4.4 17.0 1.0
CD2 A:HIS552 4.4 17.3 1.0
NE2 A:HIS424 4.4 19.4 1.0
CD2 A:HIS424 4.4 18.7 1.0
CA A:HIS552 4.5 13.7 1.0
CB A:GLU300 4.5 23.4 1.0
O A:SER553 4.6 16.5 1.0
CA A:GLU300 4.8 25.9 1.0
CA A:HIS424 4.8 16.1 1.0
N A:SER553 4.8 14.7 1.0
N A:HIS424 4.9 16.5 1.0
CZ A:ARG482 4.9 15.9 1.0

Reference:

D.Reverter, C.Fernandez-Catalan, R.Baumgartner, R.Pfander, R.Huber, W.Bode, J.Vendrell, T.A.Holak, F.X.Aviles. Structure of A Novel Leech Carboxypeptidase Inhibitor Determined Free in Solution and in Complex with Human Carboxypeptidase A2. Nat.Struct.Biol. V. 7 322 2000.
ISSN: ISSN 1072-8368
PubMed: 10742178
DOI: 10.1038/74092
Page generated: Sat Oct 12 23:51:10 2024

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