Atomistry » Zinc » PDB 1ed8-1evl » 1efz
Atomistry »
  Zinc »
    PDB 1ed8-1evl »
      1efz »

Zinc in PDB 1efz: Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity

Enzymatic activity of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity

All present enzymatic activity of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity:
2.4.2.29;

Protein crystallography data

The structure of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity, PDB code: 1efz was solved by U.Gradler, R.Ficner, G.A.Garcia, M.T.Stubbs, G.Klebe, K.Reuter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 71.00 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.600, 65.040, 70.740, 90.00, 96.25, 90.00
R / Rfree (%) 16.1 / 19.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity (pdb code 1efz). 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 Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity, PDB code: 1efz:

Zinc binding site 1 out of 1 in 1efz

Go back to Zinc Binding Sites List in 1efz
Zinc binding site 1 out of 1 in the Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:17.3
occ:1.00
 ND1 A:HIS349 2.2 9.9 1.0
SG A:CYS318 2.3 17.0 1.0
SG A:CYS323 2.3 14.6 1.0
SG A:CYS320 2.3 12.8 1.0
CE1 A:HIS349 3.0 12.6 1.0
CB A:CYS318 3.1 16.1 1.0
CG A:HIS349 3.3 8.3 1.0
CB A:CYS323 3.3 12.8 1.0
CB A:CYS320 3.3 11.0 1.0
CB A:HIS349 3.8 9.7 1.0
N A:CYS323 3.9 13.2 1.0
CA A:HIS349 4.1 10.3 1.0
N A:CYS320 4.1 16.1 1.0
NE2 A:HIS349 4.2 12.6 1.0
CA A:CYS320 4.2 13.1 1.0
CA A:CYS323 4.2 14.4 1.0
CD2 A:HIS349 4.3 10.4 1.0
CA A:CYS318 4.5 20.5 1.0
O A:HIS349 4.5 11.1 1.0
O A:CYS320 4.6 10.4 1.0
C A:CYS320 4.6 11.2 1.0
C A:CYS318 4.7 20.2 1.0
C A:HIS349 4.7 11.9 1.0
CB A:VAL322 4.8 13.7 1.0
O A:CYS318 4.9 20.2 1.0
C A:VAL322 5.0 14.2 1.0

Reference:

U.Gradler, R.Ficner, G.A.Garcia, M.T.Stubbs, G.Klebe, K.Reuter. Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna-Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity. Febs Lett. V. 454 142 1999.
ISSN: ISSN 0014-5793
PubMed: 10413112
DOI: 10.1016/S0014-5793(99)00793-0
Page generated: Sun Oct 13 00:13:21 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