Atomistry » Zinc » PDB 1oht-1p0f » 1p0d
Atomistry »
  Zinc »
    PDB 1oht-1p0f »
      1p0d »

Zinc in PDB 1p0d: Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Crystallised at pH 5.5

Enzymatic activity of Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Crystallised at pH 5.5

All present enzymatic activity of Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Crystallised at pH 5.5:
2.4.2.29;

Protein crystallography data

The structure of Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Crystallised at pH 5.5, PDB code: 1p0d 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) 32.69 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.380, 65.370, 70.570, 90.00, 96.30, 90.00
R / Rfree (%) 17.2 / 20.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Crystallised at pH 5.5 (pdb code 1p0d). 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 Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Crystallised at pH 5.5, PDB code: 1p0d:

Zinc binding site 1 out of 1 in 1p0d

Go back to Zinc Binding Sites List in 1p0d
Zinc binding site 1 out of 1 in the Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Crystallised 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 Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Crystallised at pH 5.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:18.0
occ:1.00
 ND1 A:HIS349 2.2 13.9 1.0
SG A:CYS323 2.3 13.6 1.0
SG A:CYS318 2.4 17.0 1.0
SG A:CYS320 2.4 14.7 1.0
CE1 A:HIS349 3.1 16.9 1.0
CB A:CYS318 3.2 19.9 1.0
CG A:HIS349 3.3 13.9 1.0
CB A:CYS320 3.3 13.6 1.0
CB A:CYS323 3.3 15.8 1.0
CB A:HIS349 3.7 13.5 1.0
N A:CYS323 3.9 17.3 1.0
CA A:HIS349 4.1 13.3 1.0
N A:CYS320 4.1 18.6 1.0
CA A:CYS320 4.2 16.5 1.0
CA A:CYS323 4.2 15.9 1.0
NE2 A:HIS349 4.2 14.6 1.0
CD2 A:HIS349 4.4 15.4 1.0
O A:HIS349 4.5 11.4 1.0
CA A:CYS318 4.6 20.2 1.0
O A:CYS320 4.6 15.3 1.0
C A:CYS320 4.7 16.5 1.0
C A:CYS318 4.7 21.1 1.0
C A:HIS349 4.7 13.7 1.0
CB A:VAL322 4.7 16.3 1.0
O A:CYS318 4.9 20.9 1.0
C A:VAL322 4.9 17.8 1.0
CB A:LEU314 5.0 18.1 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 17:39:33 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy