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
|