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Zinc in PDB 3uvi: Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant

Enzymatic activity of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant

All present enzymatic activity of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant, PDB code: 3uvi was solved by S.Jakobi, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.08 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.019, 64.984, 70.488, 90.00, 95.60, 90.00
R / Rfree (%) 16.5 / 19.1

Other elements in 3uvi:

The structure of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant also contains other interesting chemical elements:

Iodine (I) 10 atoms
Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant (pdb code 3uvi). 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 Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant, PDB code: 3uvi:

Zinc binding site 1 out of 1 in 3uvi

Go back to Zinc Binding Sites List in 3uvi
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Trna-Guanine Transglycosylase C158S C281S W326E E339Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn387

b:11.1
occ:1.00
ND1 A:HIS349 2.1 9.1 1.0
SG A:CYS318 2.3 12.2 1.0
SG A:CYS323 2.3 10.4 1.0
SG A:CYS320 2.4 9.6 1.0
CE1 A:HIS349 2.9 10.9 1.0
CB A:CYS318 3.2 12.2 1.0
CG A:HIS349 3.2 7.8 1.0
CB A:CYS323 3.3 10.5 1.0
CB A:CYS320 3.4 9.7 1.0
CB A:HIS349 3.7 10.2 1.0
N A:CYS323 3.9 10.6 1.0
NE2 A:HIS349 4.1 9.4 1.0
CA A:HIS349 4.1 7.4 1.0
N A:CYS320 4.2 11.7 1.0
CA A:CYS323 4.2 10.7 1.0
CA A:CYS320 4.2 9.8 1.0
CD2 A:HIS349 4.3 10.6 1.0
O A:HIS349 4.5 9.2 1.0
CA A:CYS318 4.6 12.2 1.0
C A:CYS318 4.7 13.7 1.0
O A:CYS320 4.7 13.1 1.0
C A:CYS320 4.7 10.9 1.0
C A:HIS349 4.8 8.4 1.0
CB A:VAL322 4.8 10.0 1.0
O A:CYS318 4.8 15.6 1.0
C A:VAL322 4.9 13.2 1.0

Reference:

S.Jakobi, T.X.Nguyen, F.Debaene, A.Metz, S.Sanglier-Cianferani, K.Reuter, G.Klebe. Hot-Spot Analysis to Dissect the Functional Protein-Protein Interface of A Trna-Modifying Enzyme. Proteins V. 82 2713 2014.
ISSN: ISSN 0887-3585
PubMed: 24975703
DOI: 10.1002/PROT.24637
Page generated: Wed Dec 16 04:55:09 2020

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