Zinc in PDB 1ht0: Human Gamma-2 Alcohol Dehydrogense
Enzymatic activity of Human Gamma-2 Alcohol Dehydrogense
All present enzymatic activity of Human Gamma-2 Alcohol Dehydrogense:
1.1.1.1;
Protein crystallography data
The structure of Human Gamma-2 Alcohol Dehydrogense, PDB code: 1ht0
was solved by
M.S.Niederhut,
B.J.Gibbons,
S.Perez-Miller,
T.D.Hurley,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
44.00 /
2.00
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
56.400,
71.500,
92.100,
90.00,
102.90,
90.00
|
R / Rfree (%)
|
19.3 /
23.1
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Human Gamma-2 Alcohol Dehydrogense
(pdb code 1ht0). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Human Gamma-2 Alcohol Dehydrogense, PDB code: 1ht0:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 1ht0
Go back to
Zinc Binding Sites List in 1ht0
Zinc binding site 1 out
of 4 in the Human Gamma-2 Alcohol Dehydrogense
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Human Gamma-2 Alcohol Dehydrogense within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1375
b:23.8
occ:1.00
|
SG
|
A:CYS103
|
2.2
|
18.6
|
1.0
|
SG
|
A:CYS111
|
2.4
|
18.1
|
1.0
|
SG
|
A:CYS97
|
2.4
|
19.4
|
1.0
|
SG
|
A:CYS100
|
2.5
|
18.7
|
1.0
|
CB
|
A:CYS111
|
3.3
|
19.6
|
1.0
|
CB
|
A:CYS103
|
3.3
|
20.4
|
1.0
|
CB
|
A:CYS97
|
3.3
|
22.5
|
1.0
|
N
|
A:CYS97
|
3.5
|
20.3
|
1.0
|
CB
|
A:CYS100
|
3.5
|
20.0
|
1.0
|
CA
|
A:CYS111
|
3.7
|
19.1
|
1.0
|
N
|
A:GLY98
|
3.8
|
21.9
|
1.0
|
CA
|
A:CYS97
|
3.8
|
22.4
|
1.0
|
N
|
A:CYS100
|
4.0
|
22.7
|
1.0
|
N
|
A:LEU112
|
4.0
|
19.4
|
1.0
|
N
|
A:CYS103
|
4.2
|
19.5
|
1.0
|
C
|
A:CYS97
|
4.2
|
22.5
|
1.0
|
CA
|
A:CYS103
|
4.3
|
21.6
|
1.0
|
C
|
A:CYS111
|
4.3
|
20.5
|
1.0
|
CA
|
A:CYS100
|
4.3
|
20.4
|
1.0
|
C
|
A:GLN96
|
4.5
|
18.7
|
1.0
|
N
|
A:LYS99
|
4.5
|
25.0
|
1.0
|
CD
|
A:LYS113
|
4.7
|
37.0
|
1.0
|
CA
|
A:GLY98
|
4.7
|
23.5
|
1.0
|
CA
|
A:GLN96
|
4.8
|
18.2
|
1.0
|
C
|
A:CYS100
|
4.9
|
18.7
|
1.0
|
O
|
A:CYS100
|
4.9
|
17.9
|
1.0
|
N
|
A:LYS113
|
4.9
|
24.1
|
1.0
|
|
Zinc binding site 2 out
of 4 in 1ht0
Go back to
Zinc Binding Sites List in 1ht0
Zinc binding site 2 out
of 4 in the Human Gamma-2 Alcohol Dehydrogense
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Human Gamma-2 Alcohol Dehydrogense within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1376
b:18.7
occ:1.00
|
NE2
|
A:HIS67
|
2.1
|
10.8
|
1.0
|
SG
|
A:CYS174
|
2.2
|
17.7
|
1.0
|
O
|
A:HOH1417
|
2.3
|
25.6
|
1.0
|
SG
|
A:CYS46
|
2.3
|
14.6
|
1.0
|
CD2
|
A:HIS67
|
3.1
|
14.2
|
1.0
|
CE1
|
A:HIS67
|
3.1
|
10.4
|
1.0
|
CB
|
A:CYS46
|
3.2
|
17.2
|
1.0
|
CB
|
A:CYS174
|
3.4
|
15.9
|
1.0
|
C5N
|
A:NAD1377
|
3.4
|
16.8
|
1.0
|
C6N
|
A:NAD1377
|
3.9
|
15.1
|
1.0
|
OG
|
A:SER48
|
4.0
|
18.5
|
1.0
|
CB
|
A:SER48
|
4.2
|
15.1
|
1.0
|
C4N
|
A:NAD1377
|
4.2
|
18.3
|
1.0
|
ND1
|
A:HIS67
|
4.3
|
12.2
|
1.0
|
CG
|
A:HIS67
|
4.3
|
13.4
|
1.0
|
O
|
A:HOH1480
|
4.4
|
25.5
|
1.0
|
NH2
|
A:ARG369
|
4.4
|
13.5
|
1.0
|
OE2
|
A:GLU68
|
4.7
|
21.5
|
1.0
|
CA
|
A:CYS46
|
4.7
|
12.5
|
1.0
|
CA
|
A:CYS174
|
4.7
|
15.9
|
1.0
|
N
|
A:GLY175
|
4.8
|
14.6
|
1.0
|
N
|
A:SER48
|
5.0
|
11.8
|
1.0
|
|
Zinc binding site 3 out
of 4 in 1ht0
Go back to
Zinc Binding Sites List in 1ht0
Zinc binding site 3 out
of 4 in the Human Gamma-2 Alcohol Dehydrogense
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Human Gamma-2 Alcohol Dehydrogense within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn2375
b:22.6
occ:1.00
|
SG
|
B:CYS103
|
2.1
|
21.0
|
1.0
|
SG
|
B:CYS97
|
2.4
|
19.8
|
1.0
|
SG
|
B:CYS111
|
2.4
|
15.2
|
1.0
|
SG
|
B:CYS100
|
2.5
|
19.2
|
1.0
|
CB
|
B:CYS111
|
3.3
|
16.8
|
1.0
|
CB
|
B:CYS103
|
3.3
|
21.1
|
1.0
|
CB
|
B:CYS97
|
3.4
|
22.6
|
1.0
|
N
|
B:CYS97
|
3.5
|
19.9
|
1.0
|
CB
|
B:CYS100
|
3.5
|
21.6
|
1.0
|
N
|
B:GLY98
|
3.8
|
20.8
|
1.0
|
CA
|
B:CYS111
|
3.8
|
18.7
|
1.0
|
CA
|
B:CYS97
|
3.9
|
21.3
|
1.0
|
N
|
B:CYS100
|
3.9
|
22.8
|
1.0
|
N
|
B:LEU112
|
4.1
|
19.9
|
1.0
|
N
|
B:CYS103
|
4.2
|
19.1
|
1.0
|
C
|
B:CYS97
|
4.2
|
21.1
|
1.0
|
CA
|
B:CYS100
|
4.3
|
20.7
|
1.0
|
CA
|
B:CYS103
|
4.3
|
20.6
|
1.0
|
C
|
B:CYS111
|
4.4
|
19.7
|
1.0
|
C
|
B:GLN96
|
4.4
|
18.5
|
1.0
|
N
|
B:LYS99
|
4.5
|
23.8
|
1.0
|
CA
|
B:GLN96
|
4.7
|
16.9
|
1.0
|
CA
|
B:GLY98
|
4.8
|
23.8
|
1.0
|
CG
|
B:LYS113
|
4.9
|
23.9
|
1.0
|
C
|
B:CYS100
|
4.9
|
19.4
|
1.0
|
N
|
B:LYS113
|
4.9
|
21.9
|
1.0
|
O
|
B:CYS100
|
5.0
|
19.0
|
1.0
|
|
Zinc binding site 4 out
of 4 in 1ht0
Go back to
Zinc Binding Sites List in 1ht0
Zinc binding site 4 out
of 4 in the Human Gamma-2 Alcohol Dehydrogense
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Human Gamma-2 Alcohol Dehydrogense within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn2376
b:18.9
occ:1.00
|
NE2
|
B:HIS67
|
2.1
|
11.6
|
1.0
|
SG
|
B:CYS174
|
2.2
|
15.8
|
1.0
|
O
|
B:HOH2682
|
2.3
|
16.4
|
1.0
|
SG
|
B:CYS46
|
2.3
|
15.1
|
1.0
|
CD2
|
B:HIS67
|
3.1
|
14.3
|
1.0
|
CE1
|
B:HIS67
|
3.1
|
10.9
|
1.0
|
CB
|
B:CYS46
|
3.2
|
14.2
|
1.0
|
CB
|
B:CYS174
|
3.3
|
15.3
|
1.0
|
C5N
|
B:NAD2377
|
3.4
|
15.4
|
1.0
|
C6N
|
B:NAD2377
|
4.0
|
12.9
|
1.0
|
OG
|
B:SER48
|
4.1
|
17.0
|
1.0
|
CB
|
B:SER48
|
4.2
|
14.3
|
1.0
|
CG
|
B:HIS67
|
4.2
|
9.4
|
1.0
|
ND1
|
B:HIS67
|
4.2
|
9.2
|
1.0
|
C4N
|
B:NAD2377
|
4.2
|
17.8
|
1.0
|
NH2
|
B:ARG369
|
4.4
|
13.2
|
1.0
|
OE2
|
B:GLU68
|
4.7
|
19.4
|
1.0
|
CA
|
B:CYS174
|
4.7
|
16.0
|
1.0
|
CA
|
B:CYS46
|
4.7
|
13.3
|
1.0
|
O
|
B:HOH2422
|
4.8
|
29.1
|
1.0
|
N
|
B:GLY175
|
4.8
|
14.3
|
1.0
|
C
|
B:CYS174
|
5.0
|
16.5
|
1.0
|
CE1
|
B:PHE93
|
5.0
|
12.8
|
1.0
|
|
Reference:
M.S.Niederhut,
B.J.Gibbons,
S.Perez-Miller,
T.D.Hurley.
Three-Dimensional Structures of the Three Human Class I Alcohol Dehydrogenases. Protein Sci. V. 10 697 2001.
ISSN: ISSN 0961-8368
PubMed: 11274460
DOI: 10.1110/PS.45001
Page generated: Sun Oct 13 02:31:23 2024
|