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Atomistry » Zinc » PDB 2a25-2aer » 2a5h | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2a25-2aer » 2a5h » |
Zinc in PDB 2a5h: 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate).Enzymatic activity of 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate).
All present enzymatic activity of 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate).:
5.4.3.2; Protein crystallography data
The structure of 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate)., PDB code: 2a5h
was solved by
B.W.Lepore,
F.J.Ruzicka,
P.A.Frey,
D.Ringe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2a5h:
The structure of 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate). also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate).
(pdb code 2a5h). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate)., PDB code: 2a5h: Jump to Zinc binding site number: 1; 2; 3; 4; Zinc binding site 1 out of 4 in 2a5hGo back to Zinc Binding Sites List in 2a5h
Zinc binding site 1 out
of 4 in the 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate).
Mono view Stereo pair view
Zinc binding site 2 out of 4 in 2a5hGo back to Zinc Binding Sites List in 2a5h
Zinc binding site 2 out
of 4 in the 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate).
Mono view Stereo pair view
Zinc binding site 3 out of 4 in 2a5hGo back to Zinc Binding Sites List in 2a5h
Zinc binding site 3 out
of 4 in the 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate).
Mono view Stereo pair view
Zinc binding site 4 out of 4 in 2a5hGo back to Zinc Binding Sites List in 2a5h
Zinc binding site 4 out
of 4 in the 2.1 Angstrom X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale SB4, with Michaelis Analog (L-Alpha-Lysine External Aldimine Form of Pyridoxal-5'-Phosphate).
Mono view Stereo pair view
Reference:
B.W.Lepore,
F.J.Ruzicka,
P.A.Frey,
D.Ringe.
The X-Ray Crystal Structure of Lysine-2,3-Aminomutase From Clostridium Subterminale. Proc.Natl.Acad.Sci.Usa V. 102 13819 2005.
Page generated: Wed Oct 16 21:30:31 2024
ISSN: ISSN 0027-8424 PubMed: 16166264 DOI: 10.1073/PNAS.0505726102 |
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