Atomistry » Zinc » PDB 3vh2-3w51 » 3vu8
Atomistry »
  Zinc »
    PDB 3vh2-3w51 »
      3vu8 »

Zinc in PDB 3vu8: Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue

Enzymatic activity of Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue

All present enzymatic activity of Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue:
6.1.1.10;

Protein crystallography data

The structure of Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue, PDB code: 3vu8 was solved by M.Konno, M.Kato-Murayama, S.Toma-Fukai, E.Uchikawa, O.Nureki, S.Yokoyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.823, 82.682, 120.165, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 30

Zinc Binding Sites:

The binding sites of Zinc atom in the Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue (pdb code 3vu8). 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 Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue, PDB code: 3vu8:

Zinc binding site 1 out of 1 in 3vu8

Go back to Zinc Binding Sites List in 3vu8
Zinc binding site 1 out of 1 in the Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metionyl-Trna Synthetase From Thermus Thermophilus Complexed with Methionyl-Adenylate Analogue within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:53.1
occ:1.00
 SG A:CYS127 2.1 39.9 1.0
SG A:CYS130 2.4 37.2 1.0
ND1 A:HIS147 2.4 31.9 1.0
SG A:CYS144 2.6 32.1 1.0
CG A:HIS147 3.1 33.6 1.0
CB A:CYS130 3.2 29.5 1.0
CB A:CYS127 3.2 37.3 1.0
CB A:HIS147 3.3 37.0 1.0
CE1 A:HIS147 3.4 31.8 1.0
N A:CYS130 3.5 27.6 1.0
CB A:CYS144 3.6 41.1 1.0
CA A:CYS130 3.8 28.1 1.0
N A:HIS147 4.1 45.0 1.0
CB A:SER129 4.2 30.1 1.0
CD2 A:HIS147 4.2 34.6 1.0
C A:SER129 4.2 31.3 1.0
NE2 A:HIS147 4.3 37.2 1.0
CA A:HIS147 4.3 42.2 1.0
NE A:ARG149 4.3 71.5 1.0
CA A:CYS127 4.6 35.4 1.0
CA A:SER129 4.6 32.3 1.0
N A:SER129 4.7 29.8 1.0
NH2 A:ARG149 4.7 75.0 1.0
C A:CYS127 4.9 33.4 1.0
CB A:ILE146 4.9 45.2 1.0
CZ A:ARG149 4.9 75.9 1.0
C A:ILE146 4.9 46.6 1.0
CG A:ARG149 5.0 63.3 1.0
CA A:CYS144 5.0 47.6 1.0
O A:SER129 5.0 34.8 1.0

Reference:

M.Konno, M.Kato-Murayama, R.Takeda, R.Takasaka, E.Uchikawa, S.Toma-Fukai, R.Ishii, O.Nureki, S.Yokoyama. The Modeling of Structures of Specific Conformation of Homosysteine-Amp Leading to Thiolactone-Formation on Class Ia Aminoacyl-Trna Synthetases To Be Published.
Page generated: Sat Oct 26 17:53:24 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