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Zinc in PDB 2oko: Z. Mobilis Trna Guanine Transglycosylase E235Q Mutant Apo-Structure at pH 5.5

Enzymatic activity of Z. Mobilis Trna Guanine Transglycosylase E235Q Mutant Apo-Structure at pH 5.5

All present enzymatic activity of Z. Mobilis Trna Guanine Transglycosylase E235Q Mutant Apo-Structure at pH 5.5:
2.4.2.29;

Protein crystallography data

The structure of Z. Mobilis Trna Guanine Transglycosylase E235Q Mutant Apo-Structure at pH 5.5, PDB code: 2oko was solved by N.Tidten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.407, 65.194, 70.514, 90.00, 96.36, 90.00
R / Rfree (%) 12.5 / 17.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Z. Mobilis Trna Guanine Transglycosylase E235Q Mutant Apo-Structure at pH 5.5 (pdb code 2oko). 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 Z. Mobilis Trna Guanine Transglycosylase E235Q Mutant Apo-Structure at pH 5.5, PDB code: 2oko:

Zinc binding site 1 out of 1 in 2oko

Go back to Zinc Binding Sites List in 2oko
Zinc binding site 1 out of 1 in the Z. Mobilis Trna Guanine Transglycosylase E235Q Mutant Apo-Structure at pH 5.5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Z. Mobilis Trna Guanine Transglycosylase E235Q Mutant Apo-Structure at pH 5.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:16.8
occ:1.00
ND1 A:HIS349 2.2 18.2 1.0
SG A:CYS318 2.3 18.5 1.0
SG A:CYS320 2.3 16.4 1.0
SG A:CYS323 2.3 17.6 1.0
CE1 A:HIS349 2.9 19.1 1.0
CB A:CYS318 3.3 20.6 1.0
CB A:CYS323 3.3 16.6 1.0
CG A:HIS349 3.3 14.5 1.0
CB A:CYS320 3.3 17.7 1.0
CB A:HIS349 3.8 15.0 1.0
N A:CYS323 3.9 16.0 1.0
NE2 A:HIS349 4.1 17.0 1.0
N A:CYS320 4.1 18.8 1.0
CA A:HIS349 4.1 14.4 1.0
CA A:CYS320 4.2 16.9 1.0
CA A:CYS323 4.2 16.2 1.0
CD2 A:HIS349 4.3 15.2 1.0
CA A:CYS318 4.6 19.6 1.0
O A:HIS349 4.6 15.5 1.0
C A:CYS320 4.7 16.9 1.0
O A:CYS320 4.7 18.9 1.0
C A:CYS318 4.7 17.8 1.0
C A:HIS349 4.8 14.9 1.0
CB A:VAL322 4.8 15.2 1.0
O A:CYS318 4.9 21.5 1.0
C A:VAL322 4.9 16.7 1.0

Reference:

N.Tidten, B.Stengl, A.Heine, G.A.Garcia, G.Klebe, K.Reuter. Glutamate Versus Glutamine Exchange Swaps Substrate Selectivity in Trna-Guanine Transglycosylase: Insight Into the Regulation of Substrate Selectivity By Kinetic and Crystallographic Studies. J.Mol.Biol. V. 374 764 2007.
ISSN: ISSN 0022-2836
PubMed: 17949745
DOI: 10.1016/J.JMB.2007.09.062
Page generated: Wed Dec 16 03:46:11 2020

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