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Atomistry » Magnesium » PDB 2ppq-2q0e » 2puz » |
Magnesium in PDB 2puz: Crystal Structure of Imidazolonepropionase From Agrobacterium Tumefaciens with Bound Product N-Formimino-L-GlutamateEnzymatic activity of Crystal Structure of Imidazolonepropionase From Agrobacterium Tumefaciens with Bound Product N-Formimino-L-Glutamate
All present enzymatic activity of Crystal Structure of Imidazolonepropionase From Agrobacterium Tumefaciens with Bound Product N-Formimino-L-Glutamate:
3.5.2.7; Protein crystallography data
The structure of Crystal Structure of Imidazolonepropionase From Agrobacterium Tumefaciens with Bound Product N-Formimino-L-Glutamate, PDB code: 2puz
was solved by
R.Tyagi,
S.Eswaramoorthy,
S.K.Burley,
S.Swaminathan,
New York Sgxresearch Center For Structural Genomics (Nysgxrc),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2puz:
The structure of Crystal Structure of Imidazolonepropionase From Agrobacterium Tumefaciens with Bound Product N-Formimino-L-Glutamate also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Imidazolonepropionase From Agrobacterium Tumefaciens with Bound Product N-Formimino-L-Glutamate
(pdb code 2puz). 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 Imidazolonepropionase From Agrobacterium Tumefaciens with Bound Product N-Formimino-L-Glutamate, PDB code: 2puz: Magnesium binding site 1 out of 1 in 2puzGo back to Magnesium Binding Sites List in 2puz
Magnesium binding site 1 out
of 1 in the Crystal Structure of Imidazolonepropionase From Agrobacterium Tumefaciens with Bound Product N-Formimino-L-Glutamate
Mono view Stereo pair view
Reference:
R.Tyagi,
D.Kumaran,
S.K.Burley,
S.Swaminathan.
X-Ray Structure of Imidazolonepropionase From Agrobacterium Tumefaciens at 1.87 A Resolution. Proteins V. 69 652 2007.
Page generated: Wed Aug 14 02:18:35 2024
ISSN: ISSN 0887-3585 PubMed: 17640072 DOI: 10.1002/PROT.21559 |
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