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Cobalt in PDB 3ao0: Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol

Enzymatic activity of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol

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

Protein crystallography data

The structure of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol, PDB code: 3ao0 was solved by N.Shibata, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.00 / 2.25
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 243.850, 243.850, 76.806, 90.00, 90.00, 120.00
R / Rfree (%) 23.5 / 25.7

Other elements in 3ao0:

The structure of Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol also contains other interesting chemical elements:

Sodium (Na) 1 atom

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-2-Amino-1-Propanol (pdb code 3ao0). 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 (S)-2-Amino-1-Propanol, PDB code: 3ao0:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 3ao0

Go back to Cobalt Binding Sites List in 3ao0
Cobalt binding site 1 out of 2 in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-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 (S)-2-Amino-1-Propanol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co601

b:35.6
occ:1.00
CO B:B12601 0.0 35.6 1.0
N21 B:B12601 1.9 35.8 1.0
N24 B:B12601 1.9 38.4 1.0
N22 B:B12601 1.9 34.1 1.0
N23 B:B12601 1.9 31.6 1.0
N3B B:B12601 2.3 39.0 1.0
C19 B:B12601 2.8 37.3 1.0
C1 B:B12601 2.9 38.8 1.0
C14 B:B12601 2.9 31.8 1.0
C4 B:B12601 2.9 37.4 1.0
C9 B:B12601 2.9 30.7 1.0
C11 B:B12601 3.0 34.0 1.0
C16 B:B12601 3.0 34.9 1.0
C6 B:B12601 3.0 33.0 1.0
C9B B:B12601 3.3 38.4 1.0
C2B B:B12601 3.3 37.9 1.0
C10 B:B12601 3.4 30.3 1.0
C5 B:B12601 3.4 32.5 1.0
C15 B:B12601 3.4 31.5 1.0
C20 B:B12601 3.6 36.2 1.0
C4B B:B12601 3.7 43.9 1.0
C2 B:B12601 4.1 39.0 1.0
C18 B:B12601 4.1 39.5 1.0
C3 B:B12601 4.2 38.3 1.0
C13 B:B12601 4.2 32.3 1.0
C12 B:B12601 4.2 33.7 1.0
C8 B:B12601 4.3 33.7 1.0
C17 B:B12601 4.3 40.5 1.0
C7 B:B12601 4.3 35.5 1.0
N1B B:B12601 4.5 38.2 1.0
C8B B:B12601 4.5 40.1 1.0
C26 B:B12601 4.5 38.7 1.0
C42 B:B12601 4.7 32.4 1.0
C48 B:B12601 4.8 33.8 1.0
C53 B:B12601 4.9 28.5 1.0
C35 B:B12601 4.9 29.9 1.0
C46 B:B12601 5.0 33.8 1.0

Cobalt binding site 2 out of 2 in 3ao0

Go back to Cobalt Binding Sites List in 3ao0
Cobalt binding site 2 out of 2 in the Crystal Structure of Ethanolamine Ammonia-Lyase From Escherichia Coli Complexed with Cn-Cbl and (S)-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 (S)-2-Amino-1-Propanol within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Co601

b:39.6
occ:1.00
CO D:B12601 0.0 39.6 1.0
N21 D:B12601 1.9 35.0 1.0
N24 D:B12601 1.9 38.5 1.0
N22 D:B12601 1.9 40.9 1.0
N23 D:B12601 1.9 37.3 1.0
N3B D:B12601 2.4 57.2 1.0
C19 D:B12601 2.8 39.0 1.0
C1 D:B12601 2.9 42.5 1.0
C14 D:B12601 2.9 38.3 1.0
C4 D:B12601 2.9 39.5 1.0
C9 D:B12601 2.9 38.5 1.0
C11 D:B12601 3.0 40.9 1.0
C16 D:B12601 3.0 38.0 1.0
C6 D:B12601 3.0 39.4 1.0
C10 D:B12601 3.3 41.5 1.0
C2B D:B12601 3.4 57.7 1.0
C5 D:B12601 3.4 37.6 1.0
C15 D:B12601 3.4 37.2 1.0
C9B D:B12601 3.4 58.8 1.0
C20 D:B12601 3.6 43.4 1.0
C4B D:B12601 3.9 59.0 1.0
C2 D:B12601 4.1 43.1 1.0
C18 D:B12601 4.1 41.7 1.0
C3 D:B12601 4.2 41.3 1.0
C13 D:B12601 4.2 41.4 1.0
C12 D:B12601 4.2 40.5 1.0
C8 D:B12601 4.3 42.5 1.0
C17 D:B12601 4.3 41.4 1.0
C7 D:B12601 4.3 43.4 1.0
N1B D:B12601 4.6 56.0 1.0
C42 D:B12601 4.6 42.3 1.0
C8B D:B12601 4.6 58.5 1.0
C26 D:B12601 4.6 44.7 1.0
C48 D:B12601 4.8 43.3 1.0
C35 D:B12601 4.9 36.0 1.0
C53 D:B12601 4.9 42.1 1.0

Reference:

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
Page generated: Tue Jul 30 15:47:01 2024

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