Chlorine in PDB 4rrf: Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA

Enzymatic activity of Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA

All present enzymatic activity of Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA:
6.1.1.3;

Protein crystallography data

The structure of Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA, PDB code: 4rrf was solved by S.Ahmad, A.S.K.Yerabham, V.Kamarthapu, R.Sankaranarayanan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	25.00 / 1.70
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	159.595, 52.813, 98.315, 90.00, 104.04, 90.00
*R / R_free (%)*	19.4 / 23.9

Other elements in 4rrf:

The structure of Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA (pdb code 4rrf). 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 Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA, PDB code: 4rrf:

Chlorine binding site 1 out of 1 in 4rrf

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Chlorine Binding Sites List in 4rrf

Chlorine binding site 1 out of 1 in the Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Editing Domain of Threonyl-Trna Synthetase From Methanococcus Jannaschii with L-SER3AA within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl502 b:26.8 occ:1.00	NH1	A:ARG115	2.5	44.3	1.0
	CZ	A:ARG115	3.2	33.7	1.0
	N	A:PHE118	3.2	20.1	1.0
	O	A:HOH614	3.3	27.2	1.0
	O	A:HOH662	3.3	26.6	1.0
	NH2	A:ARG115	3.3	32.9	1.0
	CB	A:PHE118	3.5	18.3	1.0
	CB	A:GLU27	3.6	23.6	1.0
	CG2	A:THR29	3.7	24.8	1.0
	CG	A:GLU27	3.7	25.1	1.0
	CA	A:PRO117	4.0	18.4	1.0
	CA	A:PHE118	4.0	19.0	1.0
	C	A:PRO117	4.1	18.6	1.0
	CE	A:LYS100	4.1	27.8	1.0
	NE	A:ARG115	4.4	34.4	1.0
	CD	A:GLU27	4.6	29.7	1.0
	OE1	A:GLU27	4.6	33.6	1.0
	O	A:ALA116	4.7	19.0	1.0
	CB	A:PRO117	4.8	18.2	1.0
	O	A:HOH642	4.8	28.5	1.0
	NZ	A:LYS100	4.8	31.0	1.0
	O	A:PHE118	4.8	20.4	1.0
	CG	A:PHE118	4.9	19.6	1.0
	C	A:PHE118	5.0	18.0	1.0

Reference:

S.Ahmad, S.Muthukumar, S.K.Kuncha, S.B.Routh, A.S.Yerabham, T.Hussain, V.Kamarthapu, S.P.Kruparani, R.Sankaranarayanan. Specificity and Catalysis Hardwired at the Rna-Protein Interface in A Translational Proofreading Enzyme. Nat Commun V. 6 7552 2015.
ISSN: ESSN 2041-1723
PubMed: 26113036
DOI: 10.1038/NCOMMS8552

Page generated: Fri Jul 11 21:31:18 2025

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