Zinc in PDB 6nbb: Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev
Enzymatic activity of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev
All present enzymatic activity of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev:
1.1.1.1;
Zinc Binding Sites:
The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev
(pdb code 6nbb). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev, PDB code: 6nbb:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 6nbb
Go back to
Zinc Binding Sites List in 6nbb
Zinc binding site 1 out
of 4 in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn402
b:74.6
occ:1.00
|
NE2
|
A:HIS67
|
2.0
|
75.9
|
1.0
|
SG
|
A:CYS46
|
2.2
|
80.1
|
1.0
|
SG
|
A:CYS174
|
2.3
|
71.3
|
1.0
|
CB
|
A:CYS46
|
2.5
|
80.1
|
1.0
|
CD2
|
A:HIS67
|
2.9
|
75.9
|
1.0
|
CE1
|
A:HIS67
|
3.0
|
75.9
|
1.0
|
CB
|
A:CYS174
|
3.2
|
71.3
|
1.0
|
OE1
|
A:GLU68
|
3.3
|
75.8
|
1.0
|
CA
|
A:CYS46
|
3.9
|
80.1
|
1.0
|
CG
|
A:HIS67
|
4.0
|
75.9
|
1.0
|
ND1
|
A:HIS67
|
4.0
|
75.9
|
1.0
|
C5N
|
A:NAD401
|
4.1
|
62.3
|
1.0
|
CD
|
A:GLU68
|
4.2
|
75.8
|
1.0
|
CB
|
A:GLU68
|
4.2
|
75.8
|
1.0
|
CA
|
A:CYS174
|
4.5
|
71.3
|
1.0
|
OG
|
A:SER48
|
4.5
|
81.0
|
1.0
|
C6N
|
A:NAD401
|
4.6
|
62.3
|
1.0
|
CB
|
A:SER48
|
4.6
|
81.0
|
1.0
|
CG
|
A:GLU68
|
4.7
|
75.8
|
1.0
|
N
|
A:CYS46
|
4.7
|
80.1
|
1.0
|
C
|
A:CYS174
|
4.7
|
71.3
|
1.0
|
C
|
A:CYS46
|
4.8
|
80.1
|
1.0
|
N
|
A:GLY175
|
4.9
|
65.3
|
1.0
|
NH2
|
A:ARG369
|
4.9
|
74.0
|
1.0
|
C4N
|
A:NAD401
|
5.0
|
62.3
|
1.0
|
|
Zinc binding site 2 out
of 4 in 6nbb
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Zinc Binding Sites List in 6nbb
Zinc binding site 2 out
of 4 in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn403
b:74.6
occ:1.00
|
SG
|
A:CYS103
|
2.1
|
70.0
|
1.0
|
SG
|
A:CYS111
|
2.2
|
70.3
|
1.0
|
SG
|
A:CYS100
|
2.3
|
69.7
|
1.0
|
SG
|
A:CYS97
|
2.3
|
70.1
|
1.0
|
CB
|
A:CYS111
|
2.7
|
70.3
|
1.0
|
CA
|
A:CYS111
|
3.4
|
70.3
|
1.0
|
N
|
A:CYS97
|
3.4
|
70.1
|
1.0
|
CB
|
A:CYS97
|
3.4
|
70.1
|
1.0
|
CB
|
A:CYS100
|
3.6
|
69.7
|
1.0
|
CB
|
A:CYS103
|
3.6
|
70.0
|
1.0
|
CA
|
A:CYS97
|
4.0
|
70.1
|
1.0
|
N
|
A:LEU112
|
4.1
|
71.7
|
1.0
|
C
|
A:CYS111
|
4.3
|
70.3
|
1.0
|
N
|
A:CYS103
|
4.3
|
70.0
|
1.0
|
N
|
A:GLY98
|
4.3
|
70.9
|
1.0
|
C
|
A:GLN96
|
4.4
|
67.4
|
1.0
|
N
|
A:CYS111
|
4.5
|
70.3
|
1.0
|
CA
|
A:CYS103
|
4.5
|
70.0
|
1.0
|
CA
|
A:GLN96
|
4.5
|
67.4
|
1.0
|
O
|
A:PRO95
|
4.6
|
68.3
|
1.0
|
N
|
A:CYS100
|
4.6
|
69.7
|
1.0
|
CA
|
A:CYS100
|
4.7
|
69.7
|
1.0
|
C
|
A:CYS97
|
4.7
|
70.1
|
1.0
|
|
Zinc binding site 3 out
of 4 in 6nbb
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Zinc Binding Sites List in 6nbb
Zinc binding site 3 out
of 4 in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn402
b:96.3
occ:1.00
|
NE2
|
B:HIS67
|
2.0
|
76.7
|
1.0
|
SG
|
B:CYS46
|
2.3
|
79.8
|
1.0
|
SG
|
B:CYS174
|
2.3
|
70.7
|
1.0
|
CD2
|
B:HIS67
|
2.7
|
76.7
|
1.0
|
CB
|
B:CYS46
|
3.0
|
79.8
|
1.0
|
OE2
|
B:GLU68
|
3.1
|
76.5
|
1.0
|
CE1
|
B:HIS67
|
3.2
|
76.7
|
1.0
|
CB
|
B:CYS174
|
3.2
|
70.7
|
1.0
|
CG
|
B:GLU68
|
3.5
|
76.5
|
1.0
|
C5N
|
B:NAD401
|
3.7
|
42.0
|
1.0
|
CD
|
B:GLU68
|
3.7
|
76.5
|
1.0
|
CG
|
B:HIS67
|
4.0
|
76.7
|
1.0
|
ND1
|
B:HIS67
|
4.1
|
76.7
|
1.0
|
C6N
|
B:NAD401
|
4.3
|
42.0
|
1.0
|
CA
|
B:CYS46
|
4.4
|
79.8
|
1.0
|
OG
|
B:SER48
|
4.4
|
81.4
|
1.0
|
C4N
|
B:NAD401
|
4.5
|
42.0
|
1.0
|
CA
|
B:CYS174
|
4.5
|
70.7
|
1.0
|
CB
|
B:SER48
|
4.7
|
81.4
|
1.0
|
C
|
B:CYS174
|
4.7
|
70.7
|
1.0
|
N
|
B:GLY175
|
4.7
|
64.9
|
1.0
|
CB
|
B:GLU68
|
5.0
|
76.5
|
1.0
|
OE1
|
B:GLU68
|
5.0
|
76.5
|
1.0
|
|
Zinc binding site 4 out
of 4 in 6nbb
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Zinc Binding Sites List in 6nbb
Zinc binding site 4 out
of 4 in the Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Horse Liver Alcohol Dehydrogenase Determined Using Single-Particle Cryo-Em at 200 Kev within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn403
b:96.3
occ:1.00
|
SG
|
B:CYS103
|
2.2
|
70.4
|
1.0
|
SG
|
B:CYS111
|
2.2
|
69.9
|
1.0
|
SG
|
B:CYS100
|
2.2
|
70.7
|
1.0
|
SG
|
B:CYS97
|
2.2
|
72.0
|
1.0
|
CB
|
B:CYS100
|
3.2
|
70.7
|
1.0
|
CB
|
B:CYS111
|
3.3
|
69.9
|
1.0
|
CB
|
B:CYS103
|
3.4
|
70.4
|
1.0
|
CB
|
B:CYS97
|
3.5
|
72.0
|
1.0
|
N
|
B:CYS97
|
3.5
|
72.0
|
1.0
|
N
|
B:CYS100
|
4.0
|
70.7
|
1.0
|
CA
|
B:CYS97
|
4.0
|
72.0
|
1.0
|
N
|
B:GLY98
|
4.0
|
72.5
|
1.0
|
CA
|
B:CYS111
|
4.0
|
69.9
|
1.0
|
CA
|
B:CYS100
|
4.2
|
70.7
|
1.0
|
N
|
B:LEU112
|
4.3
|
71.7
|
1.0
|
N
|
B:CYS103
|
4.4
|
70.4
|
1.0
|
C
|
B:CYS97
|
4.5
|
72.0
|
1.0
|
NZ
|
B:LYS113
|
4.5
|
73.9
|
1.0
|
CA
|
B:CYS103
|
4.5
|
70.4
|
1.0
|
C
|
B:GLN96
|
4.6
|
68.5
|
1.0
|
C
|
B:CYS111
|
4.6
|
69.9
|
1.0
|
N
|
B:LYS99
|
4.8
|
72.4
|
1.0
|
CA
|
B:GLN96
|
4.8
|
68.5
|
1.0
|
C
|
B:CYS100
|
5.0
|
70.7
|
1.0
|
|
Reference:
M.A.Herzik Jr.,
M.Wu,
G.C.Lander.
High-Resolution Structure Determination of Sub-100 kDa Complexes Using Conventional Cryo-Em. Nat Commun V. 10 1032 2019.
ISSN: ESSN 2041-1723
PubMed: 30833564
DOI: 10.1038/S41467-019-08991-8
Page generated: Tue Oct 29 03:40:06 2024
|