Atomistry » Zinc » PDB 3q7f-3qln » 3q87
Atomistry »
  Zinc »
    PDB 3q7f-3qln »
      3q87 »

Zinc in PDB 3q87: Structure of E. Cuniculi MTQ2-TRM112 Complex Responible For the Methylation of ERF1 Translation Termination Factor

Protein crystallography data

The structure of Structure of E. Cuniculi MTQ2-TRM112 Complex Responible For the Methylation of ERF1 Translation Termination Factor, PDB code: 3q87 was solved by D.Liger, L.Mora, N.Lazar, S.Figaro, J.Henri, N.Scrima, R.H.Buckingham, H.Vantilbeurgh, V.Heurgue-Hamard, M.Graille, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.38 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.115, 74.316, 96.754, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 25.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of E. Cuniculi MTQ2-TRM112 Complex Responible For the Methylation of ERF1 Translation Termination Factor (pdb code 3q87). 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 Structure of E. Cuniculi MTQ2-TRM112 Complex Responible For the Methylation of ERF1 Translation Termination Factor, PDB code: 3q87:

Zinc binding site 1 out of 1 in 3q87

Go back to Zinc Binding Sites List in 3q87
Zinc binding site 1 out of 1 in the Structure of E. Cuniculi MTQ2-TRM112 Complex Responible For the Methylation of ERF1 Translation Termination Factor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of E. Cuniculi MTQ2-TRM112 Complex Responible For the Methylation of ERF1 Translation Termination Factor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn126

b:28.6
occ:1.00
SG A:CYS102 2.3 16.6 1.0
SG A:CYS105 2.3 18.4 1.0
SG A:CYS11 2.4 18.1 1.0
SG A:CYS14 2.4 20.9 1.0
CB A:CYS102 3.1 18.8 1.0
CB A:CYS11 3.2 13.6 1.0
CB A:CYS105 3.3 24.4 1.0
CB A:CYS14 3.5 22.5 1.0
N A:CYS105 3.7 23.7 1.0
N A:CYS14 3.9 20.1 1.0
CA A:CYS105 4.0 20.1 1.0
CA A:CYS14 4.3 26.1 1.0
OG1 A:THR18 4.5 25.3 1.0
CA A:CYS102 4.6 18.7 1.0
CA A:CYS11 4.6 11.3 1.0
CG2 A:THR18 4.7 19.0 1.0
CB A:LEU107 4.7 17.3 1.0
C A:CYS105 4.7 18.5 1.0
CD A:ARG13 4.7 37.6 1.0
CB A:ARG13 4.8 24.5 1.0
C A:MET104 4.8 34.4 1.0
CB A:MET104 4.8 20.3 1.0
N A:GLY106 4.9 18.4 1.0
C A:ARG13 4.9 26.6 1.0
N A:LEU107 5.0 17.6 1.0

Reference:

D.Liger, L.Mora, N.Lazar, S.Figaro, J.Henri, N.Scrima, R.H.Buckingham, H.Van Tilbeurgh, V.Heurgue-Hamard, M.Graille. Mechanism of Activation of Methyltransferases Involved in Translation By the TRM112 'Hub' Protein Nucleic Acids Res. 2011.
ISSN: ESSN 1362-4962
PubMed: 21478168
DOI: 10.1093/NAR/GKR176
Page generated: Wed Dec 16 04:44:47 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy