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Chlorine in PDB 2akw: Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine

Enzymatic activity of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine

All present enzymatic activity of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine:
6.1.1.20;

Protein crystallography data

The structure of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine, PDB code: 2akw was solved by O.M.Kotik-Kogan, N.A.Moor, D.E.Tworowski, M.G.Safro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.99 / 2.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 172.980, 172.980, 138.510, 90.00, 90.00, 120.00
R / Rfree (%) 22.9 / 23.4

Other elements in 2akw:

The structure of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine (pdb code 2akw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine, PDB code: 2akw:

Chlorine binding site 1 out of 1 in 2akw

Go back to Chlorine Binding Sites List in 2akw
Chlorine binding site 1 out of 1 in the Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl999

b:18.6
occ:1.00
 CL A:200999 0.0 18.6 1.0
CZ A:200999 1.8 16.3 1.0
CE1 A:200999 2.8 13.5 1.0
CE2 A:200999 2.8 13.9 1.0
O A:ALA314 3.1 30.7 1.0
CG1 A:VAL261 3.2 31.9 1.0
C A:ALA314 3.3 29.1 1.0
CB A:ALA314 3.5 27.1 1.0
CA A:ALA283 3.6 29.5 1.0
C A:ALA283 3.6 29.9 1.0
N A:GLY284 3.8 30.3 1.0
N A:PHE315 3.8 26.9 1.0
CA A:ALA314 4.0 28.5 1.0
CA A:PHE315 4.0 26.7 1.0
CD1 A:200999 4.1 10.3 1.0
CD2 A:200999 4.1 12.4 1.0
O A:ALA283 4.1 30.8 1.0
O A:GLY284 4.2 32.4 1.0
CG2 A:VAL261 4.2 29.4 1.0
O A:HOH1016 4.2 41.4 1.0
CB A:VAL261 4.3 30.8 1.0
N A:ALA314 4.4 29.2 1.0
N A:ALA283 4.4 28.2 1.0
CD2 A:PHE260 4.5 30.9 1.0
CE2 A:PHE260 4.5 28.9 1.0
CA A:GLY284 4.5 31.8 1.0
CG A:200999 4.6 15.1 1.0
CB A:ALA283 4.7 30.4 1.0
C A:GLY284 4.7 31.7 1.0
C A:PHE315 4.7 28.2 1.0
O A:GLY282 4.8 29.4 1.0
C A:GLY282 4.9 28.9 1.0

Reference:

O.M.Kotik-Kogan, N.A.Moor, D.E.Tworowski, M.G.Safro. Structural Basis For Discrimination of L-Phenylalanine From L-Tyrosine By Phenylalanyl-Trna Synthetase Structure V. 13 1799 2005.
ISSN: ISSN 0969-2126
PubMed: 16338408
DOI: 10.1016/J.STR.2005.08.013
Page generated: Thu Jul 10 21:10:29 2025

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