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Caesium in PDB 2ov4: Crystal Structure of B. Stearothermophilus Tryptophanyl Trna Synthetase in Complex with Adenosine Tetraphosphate

Enzymatic activity of Crystal Structure of B. Stearothermophilus Tryptophanyl Trna Synthetase in Complex with Adenosine Tetraphosphate

All present enzymatic activity of Crystal Structure of B. Stearothermophilus Tryptophanyl Trna Synthetase in Complex with Adenosine Tetraphosphate:
6.1.1.2;

Protein crystallography data

The structure of Crystal Structure of B. Stearothermophilus Tryptophanyl Trna Synthetase in Complex with Adenosine Tetraphosphate, PDB code: 2ov4 was solved by P.Retailleau, C.W.Carter Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 62.178, 62.178, 220.882, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 25.8

Caesium Binding Sites:

The binding sites of Caesium atom in the Crystal Structure of B. Stearothermophilus Tryptophanyl Trna Synthetase in Complex with Adenosine Tetraphosphate (pdb code 2ov4). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total only one binding site of Caesium was determined in the Crystal Structure of B. Stearothermophilus Tryptophanyl Trna Synthetase in Complex with Adenosine Tetraphosphate, PDB code: 2ov4:

Caesium binding site 1 out of 1 in 2ov4

Go back to Caesium Binding Sites List in 2ov4
Caesium binding site 1 out of 1 in the Crystal Structure of B. Stearothermophilus Tryptophanyl Trna Synthetase in Complex with Adenosine Tetraphosphate


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 1 of Crystal Structure of B. Stearothermophilus Tryptophanyl Trna Synthetase in Complex with Adenosine Tetraphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cs900

b:52.4
occ:0.30
 O A:TYR33 3.0 50.2 1.0
O A:GLN30 3.0 52.5 1.0
CE A:MET1 3.4 69.1 1.0
O A:GLN74 3.5 42.0 1.0
SD A:MET1 3.9 71.8 1.0
C A:TYR33 4.0 48.9 1.0
C A:GLN30 4.1 52.0 1.0
O A:HIS31 4.3 54.6 1.0
C A:GLN74 4.5 41.4 1.0
OE1 A:GLN74 4.5 45.6 1.0
C A:HIS31 4.5 54.6 1.0
CA A:HIS31 4.5 49.4 1.0
N A:ASN34 4.6 42.6 1.0
CA A:GLN74 4.6 34.2 1.0
CA A:ASN34 4.7 40.9 1.0
OD1 A:ASN34 4.7 80.3 1.0
CB A:GLN74 4.7 34.9 1.0
N A:HIS31 4.8 50.3 1.0
N A:TYR33 4.8 50.7 1.0
CA A:TYR33 5.0 47.4 1.0

Reference:

P.Retailleau, V.Weinreb, M.Hu, C.W.Carter Jr.. Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Adenosine-5' Tetraphosphate: Evidence For Distributed Use of Catalytic Binding Energy in Amino Acid Activation By Class I Aminoacyl-Trna Synthetases. J.Mol.Biol. V. 369 108 2007.
ISSN: ISSN 0022-2836
PubMed: 17428498
DOI: 10.1016/J.JMB.2007.01.091
Page generated: Sun Dec 13 10:55:53 2020

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