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Atomistry » Magnesium » PDB 1lnz-1mez » 1m83 » |
Magnesium in PDB 1m83: Crystal Structure of Tryptophanyl-Trna Synthetase Complexed with Atp in A Closed, Pre-Transition State ConformationEnzymatic 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:
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 1m83Go 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
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.
Page generated: Tue Aug 13 08:38:47 2024
ISSN: ISSN 0022-2836 PubMed: 12473451 DOI: 10.1016/S0022-2836(02)01156-7 |
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