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Atomistry » Cobalt » PDB 2xwq-3bbi » 3abs » |
Cobalt in PDB 3abs: Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Adeninylpentylcobalamin and EthanolamineEnzymatic activity of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Adeninylpentylcobalamin and Ethanolamine
All present enzymatic activity of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Adeninylpentylcobalamin and Ethanolamine:
4.3.1.7; Protein crystallography data
The structure of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Adeninylpentylcobalamin and Ethanolamine, PDB code: 3abs
was solved by
N.Shibata,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Adeninylpentylcobalamin and Ethanolamine
(pdb code 3abs). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Adeninylpentylcobalamin and Ethanolamine, PDB code: 3abs: Jump to Cobalt binding site number: 1; 2; Cobalt binding site 1 out of 2 in 3absGo back to![]() ![]()
Cobalt binding site 1 out
of 2 in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Adeninylpentylcobalamin and Ethanolamine
![]() Mono view ![]() Stereo pair view
Cobalt binding site 2 out of 2 in 3absGo back to![]() ![]()
Cobalt binding site 2 out
of 2 in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Adeninylpentylcobalamin and Ethanolamine
![]() Mono view ![]() Stereo pair view
Reference:
N.Shibata,
H.Tamagaki,
N.Hieda,
K.Akita,
H.Komori,
Y.Shomura,
S.Terawaki,
K.Mori,
N.Yasuoka,
Y.Higuchi,
T.Toraya.
Crystal Structures of Ethanolamine Ammonia-Lyase Complexed with Coenzyme B12 Analogs and Substrates. J.Biol.Chem. V. 285 26484 2010.
Page generated: Sun Jul 13 18:43:09 2025
ISSN: ISSN 0021-9258 PubMed: 20519496 DOI: 10.1074/JBC.M110.125112 |
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