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Zinc in PDB 3bli: Crystal Structure of the Catalytic Domain of Licms in Complexed with Pyruvate and Acetyl-Coa

Enzymatic activity of Crystal Structure of the Catalytic Domain of Licms in Complexed with Pyruvate and Acetyl-Coa

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Licms in Complexed with Pyruvate and Acetyl-Coa:
2.3.3.13;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Licms in Complexed with Pyruvate and Acetyl-Coa, PDB code: 3bli was solved by P.Zhang, J.Ma, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.29 / 2.50
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 84.990, 84.990, 115.730, 90.00, 90.00, 120.00
R / Rfree (%) 22.9 / 28.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Licms in Complexed with Pyruvate and Acetyl-Coa (pdb code 3bli). 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 Catalytic Domain of Licms in Complexed with Pyruvate and Acetyl-Coa, PDB code: 3bli:

Zinc binding site 1 out of 1 in 3bli

Go back to Zinc Binding Sites List in 3bli
Zinc binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Licms in Complexed with Pyruvate and Acetyl-Coa


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 Catalytic Domain of Licms in Complexed with Pyruvate and Acetyl-Coa within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1003

b:34.9
occ:1.00
 OD2 A:ASP17 2.2 38.4 1.0
O3 A:PYR1005 2.3 45.1 1.0
O2 A:PYR1005 2.4 45.4 1.0
O A:HOH1087 2.4 43.4 1.0
NE2 A:HIS207 2.4 21.3 1.0
NE2 A:HIS209 2.5 30.4 1.0
C2 A:PYR1005 2.9 45.8 1.0
C1 A:PYR1005 3.0 45.5 1.0
CE1 A:HIS209 3.2 28.9 1.0
CE1 A:HIS207 3.3 18.9 1.0
CG A:ASP17 3.3 39.4 1.0
CD2 A:HIS207 3.5 20.6 1.0
CD2 A:HIS209 3.6 30.3 1.0
OD1 A:ASN243 3.7 31.1 1.0
OD1 A:ASP17 3.7 42.3 1.0
O A:HOH1022 4.0 29.8 1.0
NH2 A:ARG16 4.1 27.2 1.0
O1 A:PYR1005 4.2 48.0 1.0
C3 A:PYR1005 4.2 45.2 1.0
CH3 A:ACO1004 4.4 98.4 1.0
ND1 A:HIS207 4.4 18.8 1.0
ND1 A:HIS209 4.4 29.6 1.0
CG A:HIS207 4.5 18.7 1.0
CB A:ASP17 4.6 39.0 1.0
NH1 A:ARG16 4.6 18.0 1.0
O A:ACO1004 4.6 97.0 1.0
CG A:HIS209 4.7 28.5 1.0
CG A:ASN243 4.7 29.1 1.0
CZ A:ARG16 4.8 23.7 1.0

Reference:

J.Ma, P.Zhang, Z.Zhang, M.Zha, H.Xu, G.Zhao, J.Ding. Molecular Basis of the Substrate Specificity and the Catalytic Mechanism of Citramalate Synthase From Leptospira Interrogans Biochem.J. V. 415 45 2008.
ISSN: ISSN 0264-6021
PubMed: 18498255
DOI: 10.1042/BJ20080242
Page generated: Thu Oct 24 11:33:13 2024

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