Magnesium in PDB 2qui: Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp

Enzymatic activity of Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp

All present enzymatic activity of Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp:
6.1.1.2;

Protein crystallography data

The structure of Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp, PDB code: 2qui was solved by N.Shen, J.P.Ding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.00 / 2.40
*Space group*	P 4₃ 2₁ 2
*Cell size a, b, c (Å), α, β, γ (°)*	79.700, 79.700, 383.200, 90.00, 90.00, 90.00
*R / R_free (%)*	21.1 / 23.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp (pdb code 2qui). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp, PDB code: 2qui:

Magnesium binding site 1 out of 1 in 2qui

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Magnesium Binding Sites List in 2qui

Magnesium binding site 1 out of 1 in the Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structures of Human Tryptophanyl-Trna Synthetase in Complex with Tryptophanamide and Atp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg500 b:75.0 occ:1.00	O2A	A:ATP502	2.7	0.4	1.0
	OG	A:SER165	2.8	48.6	1.0
	O1B	A:ATP502	2.8	0.7	1.0
	NZ	A:LYS200	2.9	46.7	1.0
	O	A:HOH622	3.5	58.0	1.0
	CZ3	A:TRP88	3.7	0.9	1.0
	CE	A:LYS200	3.8	45.6	1.0
	CB	A:SER165	3.9	44.2	1.0
	PA	A:ATP502	3.9	0.7	1.0
	O3A	A:ATP502	4.0	1.0	1.0
	PB	A:ATP502	4.0	0.2	1.0
	CE3	A:TRP88	4.0	0.5	1.0
	CD	A:LYS200	4.2	41.5	1.0
	C5'	A:ATP502	4.5	0.1	1.0
	CD	A:LYS204	4.7	62.0	1.0
	O5'	A:ATP502	4.7	0.9	1.0
	O1G	A:ATP502	4.8	0.6	1.0
	O3G	A:ATP502	4.8	0.1	1.0
	CH2	A:TRP88	4.9	0.7	1.0
	O2B	A:ATP502	4.9	0.8	1.0

Reference:

N.Shen, M.Zhou, B.Yang, Y.Yu, X.Dong, J.Ding. Catalytic Mechanism of the Tryptophan Activation Reaction Revealed By Crystal Structures of Human Tryptophanyl-Trna Synthetase in Different Enzymatic States Nucleic Acids Res. V. 36 1288 2008.
ISSN: ISSN 0305-1048
PubMed: 18180246
DOI: 10.1093/NAR/GKM1153

Page generated: Wed Aug 14 03:10:25 2024

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