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Manganese in PDB 2aly: Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with 5'-O-[N-(L-Tyrosyl)Sulphamoyl]Adenosine

Enzymatic activity of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with 5'-O-[N-(L-Tyrosyl)Sulphamoyl]Adenosine

All present enzymatic activity of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with 5'-O-[N-(L-Tyrosyl)Sulphamoyl]Adenosine:
6.1.1.20;

Protein crystallography data

The structure of Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with 5'-O-[N-(L-Tyrosyl)Sulphamoyl]Adenosine, PDB code: 2aly 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) 24.59 / 2.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 173.640, 173.640, 139.810, 90.00, 90.00, 120.00
R / Rfree (%) 22.8 / 24.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with 5'-O-[N-(L-Tyrosyl)Sulphamoyl]Adenosine (pdb code 2aly). 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 5'-O-[N-(L-Tyrosyl)Sulphamoyl]Adenosine, PDB code: 2aly:

Manganese binding site 1 out of 1 in 2aly

Go back to Manganese Binding Sites List in 2aly
Manganese binding site 1 out of 1 in the Crystal Structure of T.Thermophilus Phenylalanyl-Trna Synthetase Complexed with 5'-O-[N-(L-Tyrosyl)Sulphamoyl]Adenosine


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 5'-O-[N-(L-Tyrosyl)Sulphamoyl]Adenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn901

b:43.6
occ:1.00
 OE1 B:GLU461 2.6 32.8 1.0
OE2 A:GLU262 2.6 29.7 1.0
OD2 B:ASP452 3.3 27.0 1.0
CD A:GLU262 3.5 28.8 1.0
O B:ASP452 3.5 31.7 1.0
OD1 B:ASP458 3.7 18.4 1.0
OE1 A:GLU262 3.7 30.3 1.0
CD B:GLU461 3.8 25.9 1.0
CG B:ASP452 4.1 27.4 1.0
CB B:ASP452 4.1 27.2 1.0
CD2 B:LEU453 4.3 20.1 1.0
ND2 B:ASN163 4.3 25.0 1.0
CG B:ASP458 4.3 23.7 1.0
CB B:ASP458 4.4 22.7 1.0
OE2 B:GLU462 4.5 29.2 1.0
C B:ASP452 4.5 29.1 1.0
CA B:ASP458 4.6 25.6 1.0
OE2 B:GLU461 4.6 22.3 1.0
O B:ASP458 4.7 28.7 1.0
O B:HOH937 4.8 43.8 1.0
CG A:GLU262 4.8 27.8 1.0
CG B:GLU461 4.8 23.1 1.0
NH2 B:ARG450 4.9 30.2 1.0
CB B:GLU461 4.9 24.2 1.0
CA B:ASP452 5.0 28.5 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 13:26:55 2024

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