Atomistry » Zinc » PDB 3h67-3hi2 » 3h99
Atomistry »
  Zinc »
    PDB 3h67-3hi2 »
      3h99 »

Zinc in PDB 3h99: Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Methionine

Enzymatic activity of Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Methionine

All present enzymatic activity of Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Methionine:
6.1.1.10;

Protein crystallography data

The structure of Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Methionine, PDB code: 3h99 was solved by E.Schmitt, I.C.Tanrikulu, T.H.Yoo, M.Panvert, D.A.Tirrell, Y.Mechulam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.172, 45.293, 85.967, 90.00, 107.25, 90.00
R / Rfree (%) 16.8 / 18

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Methionine (pdb code 3h99). 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 A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Methionine, PDB code: 3h99:

Zinc binding site 1 out of 1 in 3h99

Go back to Zinc Binding Sites List in 3h99
Zinc binding site 1 out of 1 in the Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Methionine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:5.8
occ:1.00
 SG A:CYS145 2.3 5.4 1.0
SG A:CYS161 2.3 6.0 1.0
SG A:CYS148 2.3 5.2 1.0
SG A:CYS158 2.4 6.2 1.0
CB A:CYS158 3.0 7.0 1.0
CB A:CYS145 3.1 4.8 1.0
CB A:CYS161 3.3 5.8 1.0
CB A:CYS148 3.4 6.6 1.0
CG2 A:VAL160 3.6 14.5 1.0
N A:CYS148 3.7 6.3 1.0
N A:CYS161 3.8 7.2 1.0
CA A:CYS161 4.1 7.7 1.0
CA A:CYS148 4.1 6.0 1.0
CA A:CYS158 4.5 5.9 1.0
CA A:CYS145 4.6 3.9 1.0
CB A:ALA163 4.6 8.4 1.0
CB A:SER150 4.7 6.1 1.0
CB A:LYS147 4.7 10.2 1.0
C A:CYS161 4.8 7.0 1.0
C A:CYS148 4.8 6.3 1.0
N A:LYS149 4.8 5.3 1.0
N A:GLY162 4.8 6.6 1.0
OG A:SER150 4.8 7.9 1.0
C A:LYS147 4.9 7.9 1.0
N A:SER150 4.9 4.9 1.0
N A:ALA163 4.9 8.2 1.0
C A:VAL160 4.9 8.2 1.0
CB A:VAL160 5.0 8.1 1.0

Reference:

E.Schmitt, I.C.Tanrikulu, T.H.Yoo, M.Panvert, D.A.Tirrell, Y.Mechulam. Switching From An Induced-Fit to A Lock-and-Key Mechanism in An Aminoacyl-Trna Synthetase with Modified Specificity. J.Mol.Biol. V. 394 843 2009.
ISSN: ISSN 0022-2836
PubMed: 19837083
DOI: 10.1016/J.JMB.2009.10.016
Page generated: Thu Oct 24 14:20:41 2024

Last articles

Zn in 9FD2
Zn in 9GUW
Zn in 9GUX
Zn in 9F7C
Zn in 9GUR
Zn in 9F7A
Zn in 9DDE
Zn in 9DBY
Zn in 9EBZ
Zn in 9DGG
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy