Cobalt in PDB 3any: Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (R)-2-Amino-1-Propanol

All present enzymatic activity of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (R)-2-Amino-1-Propanol:
4.3.1.7;

The structure of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (R)-2-Amino-1-Propanol, PDB code: 3any was solved by N.Shibata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.84 / 2.10
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	244.073, 244.073, 76.980, 90.00, 90.00, 120.00
R / Rfree (%)	24.6 / 27.6

The binding sites of Cobalt atom in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (R)-2-Amino-1-Propanol (pdb code 3any). 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 Cn-Cbl and (R)-2-Amino-1-Propanol, PDB code: 3any:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (R)-2-Amino-1-Propanol


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (R)-2-Amino-1-Propanol within 5.0Å range: probe atom residue distance (Å) B Occ B:Co601 b:36.6 occ:1.00 CO B:B12601 0.0 36.6 1.0 N21 B:B12601 1.9 34.5 1.0 N24 B:B12601 1.9 35.1 1.0 N22 B:B12601 1.9 33.9 1.0 N23 B:B12601 1.9 28.4 1.0 N3B B:B12601 2.3 34.0 1.0 C19 B:B12601 2.8 37.1 1.0 C1 B:B12601 2.9 35.5 1.0 C14 B:B12601 2.9 33.7 1.0 C4 B:B12601 2.9 34.5 1.0 C9 B:B12601 2.9 31.2 1.0 C16 B:B12601 3.0 33.5 1.0 C11 B:B12601 3.0 34.8 1.0 C6 B:B12601 3.0 32.1 1.0 C9B B:B12601 3.3 32.8 1.0 C2B B:B12601 3.3 32.5 1.0 C10 B:B12601 3.4 30.1 1.0 C5 B:B12601 3.4 29.9 1.0 C15 B:B12601 3.4 31.2 1.0 C20 B:B12601 3.7 35.1 1.0 C4B B:B12601 3.7 36.4 1.0 C2 B:B12601 4.1 38.8 1.0 C18 B:B12601 4.1 36.0 1.0 C13 B:B12601 4.2 31.5 1.0 C3 B:B12601 4.2 35.7 1.0 C12 B:B12601 4.2 31.9 1.0 C8 B:B12601 4.3 32.9 1.0 C17 B:B12601 4.3 36.4 1.0 C7 B:B12601 4.3 34.7 1.0 N1B B:B12601 4.4 34.2 1.0 C8B B:B12601 4.5 31.9 1.0 C26 B:B12601 4.5 38.6 1.0 C42 B:B12601 4.7 31.9 1.0 C48 B:B12601 4.8 35.4 1.0 C53 B:B12601 4.9 33.4 1.0 C35 B:B12601 4.9 33.5 1.0 C46 B:B12601 4.9 33.5 1.0

Cobalt binding site 2 out of 2 in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (R)-2-Amino-1-Propanol


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (R)-2-Amino-1-Propanol within 5.0Å range: probe atom residue distance (Å) B Occ D:Co601 b:40.5 occ:1.00 CO D:B12601 0.0 40.5 1.0 N24 D:B12601 1.9 36.8 1.0 N21 D:B12601 1.9 30.2 1.0 N22 D:B12601 1.9 43.5 1.0 N23 D:B12601 1.9 39.6 1.0 N3B D:B12601 2.4 47.4 1.0 C19 D:B12601 2.8 35.7 1.0 C1 D:B12601 2.9 36.0 1.0 C14 D:B12601 2.9 39.5 1.0 C4 D:B12601 2.9 35.1 1.0 C9 D:B12601 2.9 40.1 1.0 C11 D:B12601 3.0 42.6 1.0 C16 D:B12601 3.0 36.0 1.0 C6 D:B12601 3.0 34.3 1.0 C9B D:B12601 3.3 49.3 1.0 C10 D:B12601 3.3 42.7 1.0 C2B D:B12601 3.3 47.5 1.0 C5 D:B12601 3.4 34.8 1.0 C15 D:B12601 3.4 37.1 1.0 C20 D:B12601 3.6 34.9 1.0 C4B D:B12601 3.8 50.1 1.0 C2 D:B12601 4.1 38.0 1.0 C18 D:B12601 4.1 38.1 1.0 C13 D:B12601 4.2 44.3 1.0 C3 D:B12601 4.2 35.0 1.0 C12 D:B12601 4.2 42.1 1.0 C8 D:B12601 4.3 41.2 1.0 C17 D:B12601 4.3 38.5 1.0 C7 D:B12601 4.3 40.8 1.0 N1B D:B12601 4.5 45.0 1.0 C8B D:B12601 4.6 48.3 1.0 C26 D:B12601 4.6 39.6 1.0 C42 D:B12601 4.6 45.1 1.0 C48 D:B12601 4.8 44.1 1.0 C35 D:B12601 4.9 29.4 1.0 C53 D:B12601 4.9 41.1 1.0

N.Shibata, Y.Higuchi, T.Toraya. How Coenzyme B12-Dependent Ethanolamine Ammonia-Lyase Deals with Both Enantiomers of 2-Amino-1-Propanol As Substrates: Structure-Based Rationalization. Biochemistry V. 50 591 2011.
ISSN: ISSN 0006-2960
PubMed: 21142024
DOI: 10.1021/BI101696H