Chlorine in PDB 2hrk: Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub- Complexes

Enzymatic activity of Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub- Complexes

All present enzymatic activity of Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub- Complexes:
6.1.1.17;

Protein crystallography data

The structure of Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub- Complexes, PDB code: 2hrk was solved by H.Simader, D.Suck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	45.00 / 2.05
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	40.320, 86.310, 47.120, 90.00, 99.37, 90.00
*R / R_free (%)*	19.1 / 25.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub- Complexes (pdb code 2hrk). 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 Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub- Complexes, PDB code: 2hrk:

Chlorine binding site 1 out of 1 in 2hrk

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Chlorine Binding Sites List in 2hrk

Chlorine binding site 1 out of 1 in the Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub- Complexes

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub- Complexes within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl401 b:36.8 occ:1.00	CA	A:PHE81	3.5	32.4	1.0
	N	A:ILE84	3.6	32.0	1.0
	C	A:PHE81	3.6	32.5	1.0
	CB	A:ALA83	3.6	32.3	1.0
	N	A:ALA83	3.6	32.4	1.0
	CB	A:PHE81	3.7	32.3	1.0
	CG1	A:ILE84	3.7	31.2	1.0
	O	A:PHE81	3.8	32.2	1.0
	CD1	A:ILE84	3.9	31.1	1.0
	CD2	A:PHE81	4.0	32.4	1.0
	CA	A:ALA83	4.0	32.3	1.0
	N	A:ALA82	4.0	32.5	1.0
	CB	A:ILE84	4.2	31.5	1.0
	C	A:ALA83	4.2	32.3	1.0
	CG	A:PHE81	4.3	31.8	1.0
	CA	A:ILE84	4.5	31.9	1.0
	C	A:ALA82	4.6	32.5	1.0
	N	A:PHE81	4.9	32.7	1.0
	CA	A:ALA82	4.9	32.6	1.0
	O	A:LYS80	4.9	33.1	1.0
	O	A:HOH496	5.0	55.0	1.0

Reference:

H.Simader, M.Hothorn, C.Kohler, J.Basquin, G.Simos, D.Suck. Structural Basis of Yeast Aminoacyl-Trna Synthetase Complex Formation Revealed By Crystal Structures of Two Binary Sub-Complexes. Nucleic Acids Res. V. 34 3968 2006.
ISSN: ISSN 0305-1048
PubMed: 16914447
DOI: 10.1093/NAR/GKL560

Page generated: Sat Dec 12 09:07:41 2020

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