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Zinc in PDB 3ble: Crystal Structure of the Catalytic Domain of Licms in Complexed with Malonate

Enzymatic activity of Crystal Structure of the Catalytic Domain of Licms in Complexed with Malonate

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Licms in Complexed with Malonate:
2.3.3.13;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Licms in Complexed with Malonate, PDB code: 3ble 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) 39.84 / 2.00
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 85.158, 85.158, 112.897, 90.00, 90.00, 120.00
R / Rfree (%) 22.3 / 25.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Catalytic Domain of Licms in Complexed with Malonate (pdb code 3ble). 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 Malonate, PDB code: 3ble:

Zinc binding site 1 out of 1 in 3ble

Go back to Zinc Binding Sites List in 3ble
Zinc binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Licms in Complexed with Malonate


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 Malonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1003

b:35.9
occ:1.00
O6 A:MLI701 2.1 36.9 1.0
NE2 A:HIS207 2.2 26.8 1.0
NE2 A:HIS209 2.2 30.9 1.0
O9 A:MLI701 2.3 39.4 1.0
O A:HOH1047 2.4 26.6 1.0
C2 A:MLI701 2.9 37.8 1.0
CE1 A:HIS209 3.0 31.5 1.0
CD2 A:HIS207 3.0 27.0 1.0
C3 A:MLI701 3.1 38.2 1.0
C1 A:MLI701 3.2 37.3 1.0
CE1 A:HIS207 3.3 26.7 1.0
O A:HOH1102 3.3 48.1 1.0
CD2 A:HIS209 3.4 26.8 1.0
OD1 A:ASN243 3.8 24.9 1.0
O7 A:MLI701 4.1 36.7 1.0
O A:HOH1109 4.1 39.1 1.0
ND1 A:HIS209 4.2 29.3 1.0
NH2 A:ARG16 4.2 31.2 1.0
CG A:HIS207 4.2 27.2 1.0
OD2 A:ASP17 4.3 38.8 1.0
ND1 A:HIS207 4.3 27.2 1.0
O8 A:MLI701 4.3 40.3 1.0
NH1 A:ARG16 4.4 28.1 1.0
CG A:HIS209 4.4 26.9 1.0
CZ A:ARG16 4.8 31.6 1.0
CG A:ASN243 4.9 23.0 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: Wed Dec 16 04:09:12 2020

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