Manganese in PDB 2akw: Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine

Enzymatic activity of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine

All present enzymatic activity of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine:
6.1.1.20;

Protein crystallography data

The structure of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine, PDB code: 2akw was solved by O.M.Kotik-Kogan, N.A.Moor, D.E.Tworowski, M.G.Safro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	9.99 / 2.80
*Space group*	P 3₂ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	172.980, 172.980, 138.510, 90.00, 90.00, 120.00
*R / R_free (%)*	22.9 / 23.4

Other elements in 2akw:

The structure of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine (pdb code 2akw). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine, PDB code: 2akw:

Manganese binding site 1 out of 1 in 2akw

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Manganese Binding Sites List in 2akw

Manganese binding site 1 out of 1 in the Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine

Mono view

Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with P-Cl-Phenylalanine within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mn901 b:43.0 occ:1.00	OE1	B:GLU461	2.6	33.4	1.0
	OE2	A:GLU262	2.7	43.4	1.0
	CD	A:GLU262	3.4	40.4	1.0
	OE1	A:GLU262	3.5	43.7	1.0
	OD2	B:ASP452	3.6	31.6	1.0
	CD	B:GLU461	3.7	31.3	1.0
	OD1	B:ASP458	4.0	28.7	1.0
	OE2	B:GLU462	4.1	34.9	1.0
	O	B:ASP452	4.2	35.4	1.0
	OE2	B:GLU461	4.3	30.7	1.0
	ND2	B:ASN163	4.3	29.4	1.0
	O	B:ASP458	4.4	30.9	1.0
	CB	B:GLU461	4.5	26.8	1.0
	CG	B:ASP452	4.6	33.6	1.0
	CD2	B:LEU453	4.6	27.3	1.0
	CG	B:GLU461	4.6	27.1	1.0
	CA	B:ASP458	4.7	29.7	1.0
	CB	B:ASP452	4.7	32.1	1.0
	CG	B:ASP458	4.7	30.7	1.0
	CG	A:GLU262	4.7	38.5	1.0
	CB	B:ASP458	4.8	28.3	1.0
	O	B:HOH825	5.0	42.2	1.0

Reference:

O.M.Kotik-Kogan, N.A.Moor, D.E.Tworowski, M.G.Safro. Structural Basis For Discrimination of L-Phenylalanine From L-Tyrosine By Phenylalanyl-Trna Synthetase Structure V. 13 1799 2005.
ISSN: ISSN 0969-2126
PubMed: 16338408
DOI: 10.1016/J.STR.2005.08.013

Page generated: Sat Oct 5 13:26:07 2024

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