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Zinc in PDB 1ozm: Y106F Mutant of Z. Mobilis Tgt

Enzymatic activity of Y106F Mutant of Z. Mobilis Tgt

All present enzymatic activity of Y106F Mutant of Z. Mobilis Tgt:
2.4.2.29;

Protein crystallography data

The structure of Y106F Mutant of Z. Mobilis Tgt, PDB code: 1ozm was solved by R.Brenk, M.T.Stubbs, A.Heine, K.Reuter, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.95
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.390, 64.720, 71.880, 90.00, 97.02, 90.00
R / Rfree (%) 18.4 / 19.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Y106F Mutant of Z. Mobilis Tgt (pdb code 1ozm). 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 Y106F Mutant of Z. Mobilis Tgt, PDB code: 1ozm:

Zinc binding site 1 out of 1 in 1ozm

Go back to Zinc Binding Sites List in 1ozm
Zinc binding site 1 out of 1 in the Y106F Mutant of Z. Mobilis Tgt


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Y106F Mutant of Z. Mobilis Tgt within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:16.5
occ:1.00
ND1 A:HIS349 2.2 12.2 1.0
SG A:CYS323 2.3 14.5 1.0
SG A:CYS318 2.4 14.2 1.0
SG A:CYS320 2.4 13.1 1.0
CE1 A:HIS349 3.0 13.3 1.0
CB A:CYS318 3.2 13.7 1.0
CB A:CYS323 3.3 14.2 1.0
CG A:HIS349 3.3 11.1 1.0
CB A:CYS320 3.4 14.2 1.0
CB A:HIS349 3.8 10.9 1.0
N A:CYS323 3.9 12.9 1.0
N A:CYS320 4.1 14.9 1.0
CA A:HIS349 4.1 11.6 1.0
NE2 A:HIS349 4.2 14.2 1.0
CA A:CYS323 4.2 13.0 1.0
CA A:CYS320 4.2 15.9 1.0
CD2 A:HIS349 4.4 12.6 1.0
O A:HIS349 4.5 12.2 1.0
CA A:CYS318 4.5 17.2 1.0
C A:CYS318 4.6 16.2 1.0
O A:CYS320 4.6 13.9 1.0
C A:CYS320 4.7 15.6 1.0
C A:HIS349 4.8 12.0 1.0
CB A:VAL322 4.8 11.2 1.0
O A:CYS318 4.8 16.2 1.0
C A:VAL322 4.9 13.2 1.0

Reference:

R.Brenk, M.T.Stubbs, A.Heine, K.Reuter, G.Klebe. Flexible Adaptations in the Structure of the Trna-Modifying Enzyme Trna-Guanine Transglycosylase and Their Implications For Substrate Selectivity, Reaction Mechanism and Structure-Based Drug Design Chembiochem V. 4 1066 2003.
ISSN: ISSN 1439-4227
PubMed: 14523925
DOI: 10.1002/CBIC.200300644
Page generated: Wed Oct 16 17:38:28 2024

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