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Zinc in PDB 2c1c: Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors

Enzymatic activity of Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors

All present enzymatic activity of Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors:
3.4.17.2;

Protein crystallography data

The structure of Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors, PDB code: 2c1c was solved by A.Bayes, M.Comellas-Bigler, M.Rodriguez De La Vega, K.Maskos, W.Bode, F.X.Aviles, M.A.Jongsma, J.Beekwilder, J.Vendrell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.0 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.012, 58.339, 146.564, 90.00, 89.87, 90.00
R / Rfree (%) 21.46 / 29.2

Other elements in 2c1c:

The structure of Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors also contains other interesting chemical elements:

Yttrium (Y) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors (pdb code 2c1c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors, PDB code: 2c1c:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2c1c

Go back to Zinc Binding Sites List in 2c1c
Zinc binding site 1 out of 2 in the Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn625

b:20.5
occ:1.00
ND1 A:HIS69 2.0 12.3 1.0
ND1 A:HIS196 2.3 17.6 1.0
OE2 A:GLU72 2.4 20.1 1.0
OE1 A:GLU72 2.6 23.4 1.0
CD A:GLU72 2.8 20.5 1.0
CE1 A:HIS69 2.8 14.6 1.0
CG A:HIS69 3.1 14.7 1.0
CG A:HIS196 3.2 14.7 1.0
CB A:HIS196 3.3 12.2 1.0
CE1 A:HIS196 3.4 16.3 1.0
CB A:HIS69 3.6 14.4 1.0
NE2 A:HIS69 4.0 12.8 1.0
CD2 A:HIS69 4.1 12.5 1.0
CA A:HIS196 4.3 10.9 1.0
CG A:GLU72 4.3 19.2 1.0
OE1 A:GLU270 4.3 23.7 1.0
CD2 A:HIS196 4.4 15.8 1.0
O A:SER197 4.4 22.8 1.0
O A:HOH2043 4.4 18.1 1.0
NE2 A:HIS196 4.4 16.3 1.0
N A:SER197 4.5 28.5 1.0
O A:HOH2040 4.7 19.5 1.0
CG2 A:ILE68 4.9 19.4 1.0
C A:HIS196 5.0 9.7 1.0
CA A:HIS69 5.0 13.8 1.0

Zinc binding site 2 out of 2 in 2c1c

Go back to Zinc Binding Sites List in 2c1c
Zinc binding site 2 out of 2 in the Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn625

b:19.5
occ:1.00
ND1 B:HIS196 2.1 15.1 1.0
OE2 B:GLU72 2.2 11.7 1.0
ND1 B:HIS69 2.4 28.6 1.0
OE1 B:GLU72 2.4 14.2 1.0
CD B:GLU72 2.6 11.5 1.0
CG B:HIS196 3.1 17.3 1.0
CE1 B:HIS196 3.1 17.9 1.0
CG B:HIS69 3.3 26.9 1.0
CE1 B:HIS69 3.3 29.2 1.0
CB B:HIS196 3.3 12.1 1.0
CB B:HIS69 3.6 22.6 1.0
O B:SER197 4.0 25.0 1.0
CG B:GLU72 4.1 9.3 1.0
CA B:HIS196 4.2 11.0 1.0
CD2 B:HIS196 4.2 16.8 1.0
NE2 B:HIS196 4.2 16.1 1.0
NE2 B:HIS69 4.3 30.1 1.0
CD2 B:HIS69 4.3 28.3 1.0
N B:SER197 4.3 29.8 1.0
O B:HOH2039 4.4 14.7 1.0
O B:HOH2043 4.5 12.8 1.0
OE2 B:GLU270 4.6 24.3 1.0
C B:HIS196 4.8 10.8 1.0
CA B:HIS69 4.9 20.8 1.0
CB B:GLU72 4.9 12.3 1.0
N B:HIS69 5.0 22.4 1.0

Reference:

A.Bayes, M.Comellas-Bigler, M.Rodriguez De La Vega, K.Maskos, W.Bode, F.X.Aviles, M.A.Jongsma, J.Beekwilder, J.Vendrell. Structural Basis of the Resistance of An Insect Carboxypeptidase to Plant Protease Inhibitors. Proc.Natl.Acad.Sci.Usa V. 102 16602 2005.
ISSN: ISSN 0027-8424
PubMed: 16260742
DOI: 10.1073/PNAS.0505489102
Page generated: Wed Dec 16 03:18:50 2020

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