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Zinc in PDB 1f4l: Crystal Structure of the E.Coli Methionyl-Trna Synthetase Complexed with Methionine

Enzymatic activity of Crystal Structure of the E.Coli Methionyl-Trna Synthetase Complexed with Methionine

All present enzymatic activity of Crystal Structure of the E.Coli Methionyl-Trna Synthetase Complexed with Methionine:
6.1.1.10;

Protein crystallography data

The structure of Crystal Structure of the E.Coli Methionyl-Trna Synthetase Complexed with Methionine, PDB code: 1f4l was solved by L.Serre, G.Verdon, T.Chonowski, N.Hervouet, C.Zelwer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.400, 45.160, 86.310, 90.00, 107.91, 90.00
R / Rfree (%) 18.2 / 23.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the E.Coli Methionyl-Trna Synthetase Complexed with Methionine (pdb code 1f4l). 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 Crystal Structure of the E.Coli Methionyl-Trna Synthetase Complexed with Methionine, PDB code: 1f4l:

Zinc binding site 1 out of 1 in 1f4l

Go back to Zinc Binding Sites List in 1f4l
Zinc binding site 1 out of 1 in the Crystal Structure of the E.Coli Methionyl-Trna Synthetase 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 Crystal Structure of the E.Coli Methionyl-Trna Synthetase Complexed with Methionine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:18.1
occ:1.00
SG A:CYS148 2.5 14.0 1.0
SG A:CYS161 2.5 15.6 1.0
SG A:CYS145 2.5 14.2 1.0
SG A:CYS158 2.6 16.1 1.0
CB A:CYS158 3.2 19.4 1.0
CB A:CYS145 3.2 21.5 1.0
CB A:CYS148 3.3 16.4 1.0
CB A:CYS161 3.4 14.7 1.0
N A:CYS161 3.7 17.3 1.0
N A:CYS148 3.8 16.7 1.0
CA A:CYS161 4.0 15.4 1.0
CA A:CYS148 4.1 16.8 1.0
CA A:CYS158 4.6 17.0 1.0
CA A:CYS145 4.6 13.8 1.0
CB A:ALA163 4.7 22.2 1.0
C A:CYS161 4.7 16.2 1.0
CB A:LYS147 4.8 21.5 1.0
C A:VAL160 4.8 17.8 1.0
CB A:SER150 4.8 17.4 1.0
N A:GLY162 4.8 15.2 1.0
C A:CYS148 4.8 16.8 1.0
N A:ALA163 4.9 19.1 1.0
C A:LYS147 4.9 17.7 1.0
N A:LYS149 4.9 13.7 1.0
OG A:SER150 5.0 22.9 1.0
N A:SER150 5.0 17.7 1.0

Reference:

L.Serre, G.Verdon, T.Choinowski, N.Hervouet, J.L.Risler, C.Zelwer. How Methionyl-Trna Synthetase Creates Its Amino Acid Recognition Pocket Upon L-Methionine Binding. J.Mol.Biol. V. 306 863 2001.
ISSN: ISSN 0022-2836
PubMed: 11243794
DOI: 10.1006/JMBI.2001.4408
Page generated: Sun Oct 13 00:46:18 2024

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