Atomistry » Cobalt » PDB 5vtd-5zt2 » 5ysn
Atomistry »
  Cobalt »
    PDB 5vtd-5zt2 »
      5ysn »

Cobalt in PDB 5ysn: Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free

Enzymatic activity of Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free

All present enzymatic activity of Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free:
4.3.1.7;

Protein crystallography data

The structure of Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free, PDB code: 5ysn 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 / 2.00
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 242.723, 242.723, 76.573, 90.00, 90.00, 120.00
R / Rfree (%) 16.3 / 19.2

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free (pdb code 5ysn). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free, PDB code: 5ysn:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 5ysn

Go back to Cobalt Binding Sites List in 5ysn
Cobalt binding site 1 out of 2 in the Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co601

b:26.8
occ:1.00
CO B:B12601 0.0 26.8 1.0
N21 B:B12601 1.8 29.6 1.0
N23 B:B12601 1.8 29.0 1.0
N22 B:B12601 1.9 27.4 1.0
N24 B:B12601 1.9 29.2 1.0
N3B B:B12601 2.3 28.6 1.0
C19 B:B12601 2.7 30.4 1.0
C1 B:B12601 2.8 31.6 1.0
C9 B:B12601 2.8 25.6 1.0
C14 B:B12601 2.8 27.6 1.0
C4 B:B12601 2.8 27.7 1.0
C11 B:B12601 2.9 27.1 1.0
C5' A:5AD501 3.0 28.3 1.0
C6 B:B12601 3.0 24.2 1.0
C16 B:B12601 3.0 27.6 1.0
C9B B:B12601 3.2 29.3 1.0
C10 B:B12601 3.3 25.0 1.0
C2B B:B12601 3.3 26.9 1.0
C5 B:B12601 3.4 25.0 1.0
C15 B:B12601 3.4 26.6 1.0
C20 B:B12601 3.5 31.6 1.0
C4B B:B12601 3.7 26.9 1.0
C2 B:B12601 4.0 29.9 1.0
C18 B:B12601 4.1 29.1 1.0
C3 B:B12601 4.1 27.1 1.0
C13 B:B12601 4.1 26.5 1.0
C8 B:B12601 4.2 24.4 1.0
C12 B:B12601 4.2 26.2 1.0
C17 B:B12601 4.3 28.1 1.0
C7 B:B12601 4.3 24.8 1.0
C4' A:5AD501 4.4 29.3 1.0
C26 B:B12601 4.4 32.0 1.0
N1B B:B12601 4.5 27.9 1.0
C8B B:B12601 4.5 28.5 1.0
C42 B:B12601 4.8 25.2 1.0
C35 B:B12601 4.9 24.6 1.0
C48 B:B12601 4.9 27.6 1.0
C53 B:B12601 4.9 25.4 1.0
C46 B:B12601 4.9 22.3 1.0
C3' A:5AD501 5.0 32.1 1.0
C30 B:B12601 5.0 28.2 1.0

Cobalt binding site 2 out of 2 in 5ysn

Go back to Cobalt Binding Sites List in 5ysn
Cobalt binding site 2 out of 2 in the Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Ethanolamine Ammonia-Lyase, Adocbl/Substrate-Free within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Co601

b:38.9
occ:1.00
CO D:B12601 0.0 38.9 1.0
N21 D:B12601 1.8 40.6 1.0
N23 D:B12601 1.8 39.5 1.0
N22 D:B12601 1.9 42.0 1.0
N24 D:B12601 1.9 36.4 1.0
N3B D:B12601 2.3 34.9 1.0
C19 D:B12601 2.7 36.5 1.0
C1 D:B12601 2.8 38.6 1.0
C9 D:B12601 2.8 41.9 1.0
C4 D:B12601 2.8 41.5 1.0
C14 D:B12601 2.9 36.2 1.0
C11 D:B12601 2.9 39.0 1.0
C6 D:B12601 3.0 40.9 1.0
C16 D:B12601 3.0 34.2 1.0
C5' C:5AD501 3.1 38.7 1.0
C9B D:B12601 3.2 36.2 1.0
C10 D:B12601 3.3 40.5 1.0
C2B D:B12601 3.3 35.0 1.0
C5 D:B12601 3.3 40.5 1.0
C15 D:B12601 3.4 33.9 1.0
C20 D:B12601 3.6 38.2 1.0
C4B D:B12601 3.7 34.7 1.0
C2 D:B12601 4.0 39.2 1.0
C3 D:B12601 4.1 41.2 1.0
C18 D:B12601 4.1 35.3 1.0
C8 D:B12601 4.1 41.7 1.0
C13 D:B12601 4.2 33.7 1.0
C12 D:B12601 4.2 34.3 1.0
C26 D:B12601 4.3 38.3 1.0
C17 D:B12601 4.3 33.8 1.0
C7 D:B12601 4.3 40.7 1.0
C4' C:5AD501 4.4 39.1 1.0
N1B D:B12601 4.5 36.0 1.0
C8B D:B12601 4.5 37.0 1.0
C41 D:B12601 4.8 42.7 1.0
C35 D:B12601 4.8 39.0 1.0
C53 D:B12601 4.9 32.0 1.0
C46 D:B12601 4.9 30.6 1.0
C54 D:B12601 5.0 32.9 1.0
C30 D:B12601 5.0 42.1 1.0

Reference:

N.Shibata, Y.Sueyoshi, Y.Higuchi, T.Toraya. Direct Participation of A Peripheral Side Chain of A Corrin Ring in Coenzyme B12CATALYSIS. Angew. Chem. Int. Ed. Engl. V. 57 7830 2018.
ISSN: ESSN 1521-3773
PubMed: 29797764
DOI: 10.1002/ANIE.201803591
Page generated: Tue Jul 30 18:23:04 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy