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Zinc in PDB 3h9b: Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Azidonorleucine

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

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

Protein crystallography data

The structure of Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Azidonorleucine, PDB code: 3h9b 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 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.259, 45.377, 85.890, 90.00, 107.24, 90.00
R / Rfree (%) 16.5 / 18.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Azidonorleucine (pdb code 3h9b). 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 Azidonorleucine, PDB code: 3h9b:

Zinc binding site 1 out of 1 in 3h9b

Go back to Zinc Binding Sites List in 3h9b
Zinc binding site 1 out of 1 in the Structure of A Mutant Methionyl-Trna Synthetase with Modified Specificity Complexed with Azidonorleucine


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 Azidonorleucine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:6.0
occ:1.00
 SG A:CYS145 2.3 6.0 1.0
SG A:CYS161 2.3 7.1 1.0
SG A:CYS148 2.4 7.1 1.0
SG A:CYS158 2.4 6.7 1.0
CB A:CYS158 3.1 8.5 1.0
CB A:CYS145 3.1 6.0 1.0
CB A:CYS161 3.3 6.3 1.0
CB A:CYS148 3.4 8.5 1.0
CG2 A:VAL160 3.6 14.9 1.0
N A:CYS148 3.7 8.6 1.0
N A:CYS161 3.8 8.3 1.0
CA A:CYS161 4.1 8.6 1.0
CA A:CYS148 4.1 8.6 1.0
CA A:CYS158 4.5 8.3 1.0
CA A:CYS145 4.6 5.2 1.0
CB A:ALA163 4.7 10.5 1.0
CB A:LYS147 4.7 12.3 1.0
CB A:SER150 4.7 7.9 1.0
C A:CYS161 4.7 9.0 1.0
C A:CYS148 4.8 8.1 1.0
N A:LYS149 4.8 7.0 1.0
N A:GLY162 4.8 8.5 1.0
C A:LYS147 4.8 9.5 1.0
OG A:SER150 4.9 8.8 1.0
N A:SER150 4.9 6.2 1.0
N A:ALA163 4.9 10.3 1.0
C A:VAL160 5.0 9.9 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: Wed Aug 20 10:00:29 2025

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