Chlorine in PDB 5k1x: Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp

Enzymatic activity of Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp

All present enzymatic activity of Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp:
6.1.1.26;

Protein crystallography data

The structure of Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp, PDB code: 5k1x was solved by A.Weber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	43.18 / 1.95
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	102.017, 44.140, 64.309, 90.00, 100.01, 90.00
*R / R_free (%)*	19.7 / 22.7

Other elements in 5k1x:

The structure of Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp (pdb code 5k1x). 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 Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp, PDB code: 5k1x:

Chlorine binding site 1 out of 1 in 5k1x

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Chlorine Binding Sites List in 5k1x

Chlorine binding site 1 out of 1 in the Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Catalytic Domain of Polyspecific Pyrrolysyl-Trna Synthetase Mutant Y306A/N346A/C348A/Y384F in Complex with Amppnp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl506 b:51.8 occ:1.00	N	A:LEU301	3.3	28.3	1.0
	SD	A:MET344	3.4	27.4	0.6
	N	A:ALA302	3.4	27.7	1.0
	CB	A:MET300	3.4	38.1	1.0
	CB	A:ALA302	4.0	26.6	1.0
	CA	A:MET300	4.0	33.5	1.0
	CA	A:LEU301	4.1	27.2	1.0
	C	A:MET300	4.1	30.2	1.0
	CE	A:MET344	4.2	27.2	0.6
	C	A:LEU301	4.2	26.6	1.0
	CA	A:ALA302	4.2	26.9	1.0
	CB	A:LEU301	4.3	24.9	1.0
	CE	A:MET344	4.5	27.6	0.4
	CG	A:MET300	4.5	42.8	1.0
	CB	A:ALA346	4.6	23.1	1.0
	O1	A:PEG505	4.7	46.5	0.8
	SD	A:MET300	4.8	49.0	1.0
	CG	A:MET344	4.9	27.4	0.4
	SD	A:MET344	5.0	27.8	0.4

Reference:

Y.J.Lee, M.J.Schmidt, J.M.Tharp, A.Weber, A.L.Koenig, H.Zheng, J.Gao, M.L.Waters, D.Summerer, W.R.Liu. Genetically Encoded Fluorophenylalanines Enable Insights Into the Recognition of Lysine Trimethylation By An Epigenetic Reader. Chem.Commun.(Camb.) V. 52 12606 2016.
ISSN: ESSN 1364-548X
PubMed: 27711380
DOI: 10.1039/C6CC05959G

Page generated: Fri Jul 26 10:22:03 2024

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