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Zinc in PDB 1zli: Crystal Structure of the Tick Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase B

Enzymatic activity of Crystal Structure of the Tick Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase B

All present enzymatic activity of Crystal Structure of the Tick Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase B:
3.4.17.2;

Protein crystallography data

The structure of Crystal Structure of the Tick Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase B, PDB code: 1zli was solved by J.L.Arolas, G.M.Popowicz, J.Lorenzo, C.P.Sommerhoff, R.Huber, F.X.Aviles, T.A.Holak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.96 / 2.09
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 74.200, 74.200, 163.550, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 21.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Tick Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase B (pdb code 1zli). 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 Tick Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase B, PDB code: 1zli:

Zinc binding site 1 out of 1 in 1zli

Go back to Zinc Binding Sites List in 1zli
Zinc binding site 1 out of 1 in the Crystal Structure of the Tick Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase B


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 Tick Carboxypeptidase Inhibitor in Complex with Human Carboxypeptidase B within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:26.6
occ:1.00
ND1 A:HIS69 2.1 12.6 1.0
OE2 A:GLU72 2.1 14.5 1.0
ND1 A:HIS196 2.2 18.2 1.0
O B:LEU74 2.5 18.1 1.0
OE1 A:GLU72 2.7 12.7 1.0
C B:LEU74 2.7 18.5 1.0
CD A:GLU72 2.7 14.2 1.0
CE1 A:HIS69 3.0 12.0 1.0
CE1 A:HIS196 3.1 18.8 1.0
CG A:HIS69 3.2 12.9 1.0
CG A:HIS196 3.3 16.8 1.0
CB A:HIS69 3.6 13.8 1.0
CB A:HIS196 3.6 15.8 1.0
O A:HOH1902 4.0 11.9 1.0
CA B:LEU74 4.1 18.1 1.0
NE2 A:HIS69 4.1 11.1 1.0
NH1 A:ARG127 4.1 15.9 1.0
CG A:GLU72 4.2 14.3 1.0
CD2 A:HIS69 4.2 13.0 1.0
NE2 A:HIS196 4.3 17.2 1.0
O A:SER197 4.3 16.4 1.0
O A:HOH1897 4.3 14.6 1.0
CD2 A:HIS196 4.4 17.5 1.0
O A:HOH2305 4.5 17.6 1.0
CA A:HIS196 4.5 15.7 1.0
O A:HOH2306 4.7 31.1 1.0
N A:SER197 4.8 16.1 1.0
N B:LEU74 4.8 17.6 1.0
OE2 A:GLU270 4.9 19.7 1.0
CA A:HIS69 4.9 13.5 1.0
O A:HOH1895 4.9 18.1 1.0
CZ A:ARG127 4.9 17.5 1.0

Reference:

J.L.Arolas, G.M.Popowicz, J.Lorenzo, C.P.Sommerhoff, R.Huber, F.X.Aviles, T.A.Holak. The Three-Dimensional Structures of Tick Carboxypeptidase Inhibitor in Complex with A/B Carboxypeptidases Reveal A Novel Double-Headed Binding Mode J.Mol.Biol. V. 350 489 2005.
ISSN: ISSN 0022-2836
PubMed: 15961103
DOI: 10.1016/J.JMB.2005.05.015
Page generated: Wed Dec 16 03:15:55 2020

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