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Zinc in PDB 1k4h: Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-Propylsulfanylmethyl-3H-Quinazoline-4-One

Enzymatic activity of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-Propylsulfanylmethyl-3H-Quinazoline-4-One

All present enzymatic activity of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-Propylsulfanylmethyl-3H-Quinazoline-4-One:
2.4.2.29;

Protein crystallography data

The structure of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-Propylsulfanylmethyl-3H-Quinazoline-4-One, PDB code: 1k4h was solved by R.Brenk, E.A.Meyer, R.K.Castellano, M.Furler, M.T.Stubbs, G.Klebe, F.Diederich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.80 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.710, 64.990, 71.070, 90.00, 96.44, 90.00
R / Rfree (%) 19.6 / 22.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-Propylsulfanylmethyl-3H-Quinazoline-4-One (pdb code 1k4h). 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 Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-Propylsulfanylmethyl-3H-Quinazoline-4-One, PDB code: 1k4h:

Zinc binding site 1 out of 1 in 1k4h

Go back to Zinc Binding Sites List in 1k4h
Zinc binding site 1 out of 1 in the Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-Propylsulfanylmethyl-3H-Quinazoline-4-One


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 Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-Propylsulfanylmethyl-3H-Quinazoline-4-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:12.3
occ:1.00
 ND1 A:HIS349 2.2 11.5 1.0
SG A:CYS323 2.3 13.7 1.0
SG A:CYS320 2.3 12.7 1.0
SG A:CYS318 2.3 13.7 1.0
CE1 A:HIS349 3.1 12.8 1.0
CB A:CYS323 3.3 12.8 1.0
CB A:CYS318 3.3 14.1 1.0
CG A:HIS349 3.4 10.9 1.0
CB A:CYS320 3.4 12.4 1.0
CB A:HIS349 3.8 11.3 1.0
N A:CYS323 3.9 12.6 1.0
N A:CYS320 4.1 13.6 1.0
CA A:HIS349 4.1 10.1 1.0
CA A:CYS323 4.2 13.3 1.0
CA A:CYS320 4.2 13.1 1.0
NE2 A:HIS349 4.2 12.1 1.0
CD2 A:HIS349 4.4 11.3 1.0
O A:HIS349 4.5 9.6 1.0
O A:CYS320 4.6 11.4 1.0
CA A:CYS318 4.6 15.9 1.0
C A:CYS318 4.7 16.4 1.0
C A:CYS320 4.7 11.7 1.0
C A:HIS349 4.8 10.4 1.0
CB A:VAL322 4.8 9.7 1.0
O A:CYS318 4.8 17.2 1.0
C A:VAL322 4.9 11.6 1.0

Reference:

E.A.Meyer, R.Brenk, R.K.Castellano, M.Furler, G.Klebe, F.Diederich. De Novo Design, Synthesis, and in Vitro Evaluation of Inhibitors For Prokaryotic Trna-Guanine Transglycosylase: A Dramatic Sulfur Effect on Binding Affinity. Chembiochem V. 3 250 2002.
ISSN: ISSN 1439-4227
PubMed: 11921407
DOI: 10.1002/1439-7633(20020301)3:2/3<250::AID-CBIC250>3.0.CO;2-J
Page generated: Sun Oct 13 04:02:48 2024

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