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Magnesium in PDB 1m83: Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State Conformation

Enzymatic activity of Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State Conformation

All present enzymatic activity of Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State Conformation:
6.1.1.2;

Protein crystallography data

The structure of Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State Conformation, PDB code: 1m83 was solved by P.Retailleau, X.Huang, Y.Yin, M.Hu, V.Weinreb, P.Vachette, C.Vonrhein, G.Bricogne, P.Roversi, V.Ilyin, C.W.Carter Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 62.133, 62.133, 217.807, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 25.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State Conformation (pdb code 1m83). 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 Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State Conformation, PDB code: 1m83:

Magnesium binding site 1 out of 1 in 1m83

Go back to Magnesium Binding Sites List in 1m83
Magnesium binding site 1 out of 1 in the Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg500

b:22.9
occ:1.00
 O A:HOH634 2.3 24.3 1.0
O1A A:ATP400 2.3 22.8 1.0
O1G A:ATP400 2.5 22.6 1.0
O1B A:ATP400 2.7 21.2 1.0
PB A:ATP400 3.5 22.1 1.0
O3B A:ATP400 3.6 22.4 1.0
PG A:ATP400 3.6 22.6 1.0
NE2 A:GLN9 3.6 16.5 1.0
PA A:ATP400 3.6 22.7 1.0
O A:HOH529 3.7 30.4 1.0
O3A A:ATP400 3.8 23.1 1.0
OE1 A:GLN107 4.1 31.9 0.7
NZ A:LYS111 4.1 61.5 1.0
CE A:LYS111 4.2 55.9 1.0
NZ A:LYS192 4.3 16.5 1.0
NE2 A:GLN147 4.4 34.1 1.0
O3G A:ATP400 4.4 22.5 1.0
OD1 A:ASP146 4.4 33.5 1.0
O5' A:ATP400 4.5 22.7 1.0
O2A A:ATP400 4.7 23.0 1.0
O2G A:ATP400 4.7 21.8 1.0
CD A:GLN107 4.8 42.4 0.7
CE A:LYS192 4.8 13.2 1.0
OH A:TYR125 4.8 32.0 1.0
O2B A:ATP400 4.8 22.8 1.0
CD A:GLN9 4.9 24.7 1.0
OE1 A:GLN107 5.0 38.3 0.3

Reference:

P.Retailleau, X.Huang, Y.Yin, M.Hu, V.Weinreb, P.Vachette, C.Vonrhein, G.Bricogne, P.Roversi, V.Ilyin, C.W.Carter. Interconversion of Atp Binding and Conformational Free Energies By Tryptophanyl-Trna Synthetase: Structures of Atp Bound to Open and Closed, Pre-Transition-State Conformations. J.Mol.Biol. V. 325 39 2003.
ISSN: ISSN 0022-2836
PubMed: 12473451
DOI: 10.1016/S0022-2836(02)01156-7
Page generated: Tue Aug 13 08:38:47 2024

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