Zinc in PDB 1n92: Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole
Enzymatic activity of Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole
All present enzymatic activity of Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole:
1.1.1.1;
Protein crystallography data
The structure of Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole, PDB code: 1n92
was solved by
J.K.Rubach,
B.V.Plapp,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.47
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
44.200,
51.050,
93.230,
78.96,
75.47,
70.24
|
R / Rfree (%)
|
15.1 /
18.3
|
Other elements in 1n92:
The structure of Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole
(pdb code 1n92). 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 Complexed with Nad+ and 4- Iodopyrazole, PDB code: 1n92:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 1n92
Go back to
Zinc Binding Sites List in 1n92
Zinc binding site 1 out
of 4 in the Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole
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 Complexed with Nad+ and 4- Iodopyrazole within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn375
b:22.1
occ:1.00
|
NE2
|
A:HIS67
|
2.0
|
17.4
|
1.0
|
N1
|
A:PYZ378
|
2.2
|
18.6
|
1.0
|
SG
|
A:CYS174
|
2.2
|
18.6
|
1.0
|
SG
|
A:CYS46
|
2.3
|
20.2
|
1.0
|
CD2
|
A:HIS67
|
3.0
|
18.6
|
1.0
|
CE1
|
A:HIS67
|
3.1
|
18.5
|
1.0
|
C5
|
A:PYZ378
|
3.1
|
19.9
|
1.0
|
N2
|
A:PYZ378
|
3.2
|
19.3
|
1.0
|
C5N
|
A:NAJ377
|
3.2
|
15.4
|
1.0
|
CB
|
A:CYS46
|
3.3
|
18.3
|
1.0
|
CB
|
A:CYS174
|
3.4
|
15.5
|
1.0
|
C4N
|
A:NAJ377
|
3.7
|
16.0
|
1.0
|
C6N
|
A:NAJ377
|
4.1
|
14.6
|
1.0
|
OG
|
A:SER48
|
4.1
|
18.6
|
1.0
|
CG
|
A:HIS67
|
4.1
|
17.0
|
1.0
|
ND1
|
A:HIS67
|
4.2
|
17.3
|
1.0
|
CB
|
A:SER48
|
4.2
|
19.1
|
1.0
|
C4
|
A:PYZ378
|
4.3
|
19.3
|
1.0
|
C3
|
A:PYZ378
|
4.4
|
20.6
|
1.0
|
NH2
|
A:ARG369
|
4.5
|
20.1
|
1.0
|
CE2
|
A:PHE93
|
4.5
|
14.7
|
1.0
|
CA
|
A:CYS174
|
4.7
|
16.0
|
1.0
|
CZ
|
A:PHE93
|
4.8
|
15.5
|
1.0
|
CA
|
A:CYS46
|
4.8
|
19.5
|
1.0
|
OE2
|
A:GLU68
|
4.9
|
19.6
|
1.0
|
|
Zinc binding site 2 out
of 4 in 1n92
Go back to
Zinc Binding Sites List in 1n92
Zinc binding site 2 out
of 4 in the Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole
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 Complexed with Nad+ and 4- Iodopyrazole within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn376
b:20.1
occ:1.00
|
SG
|
A:CYS100
|
2.3
|
19.6
|
1.0
|
SG
|
A:CYS97
|
2.3
|
21.0
|
1.0
|
SG
|
A:CYS111
|
2.3
|
18.1
|
1.0
|
SG
|
A:CYS103
|
2.4
|
16.7
|
1.0
|
CB
|
A:CYS111
|
3.3
|
16.6
|
1.0
|
CB
|
A:CYS100
|
3.4
|
19.8
|
1.0
|
CB
|
A:CYS103
|
3.4
|
17.7
|
1.0
|
CB
|
A:CYS97
|
3.4
|
18.4
|
1.0
|
N
|
A:CYS97
|
3.5
|
17.4
|
1.0
|
CA
|
A:CYS111
|
3.8
|
16.8
|
1.0
|
N
|
A:CYS100
|
3.8
|
21.1
|
1.0
|
CA
|
A:CYS97
|
3.9
|
19.7
|
1.0
|
N
|
A:LEU112
|
3.9
|
16.9
|
1.0
|
N
|
A:GLY98
|
4.0
|
20.7
|
1.0
|
CA
|
A:CYS100
|
4.2
|
20.5
|
1.0
|
N
|
A:CYS103
|
4.2
|
16.9
|
1.0
|
C
|
A:CYS111
|
4.3
|
17.1
|
1.0
|
C
|
A:CYS97
|
4.4
|
20.5
|
1.0
|
CA
|
A:CYS103
|
4.4
|
17.1
|
1.0
|
N
|
A:LYS99
|
4.5
|
21.9
|
1.0
|
C
|
A:GLN96
|
4.6
|
17.9
|
1.0
|
C
|
A:CYS100
|
4.8
|
20.8
|
1.0
|
N
|
A:LYS113
|
4.9
|
18.3
|
1.0
|
O
|
A:HOH753
|
4.9
|
36.4
|
1.0
|
CA
|
A:GLN96
|
4.9
|
17.4
|
1.0
|
O
|
A:CYS100
|
4.9
|
20.3
|
1.0
|
CA
|
A:GLY98
|
5.0
|
21.7
|
1.0
|
|
Zinc binding site 3 out
of 4 in 1n92
Go back to
Zinc Binding Sites List in 1n92
Zinc binding site 3 out
of 4 in the Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole
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 Complexed with Nad+ and 4- Iodopyrazole within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn375
b:18.5
occ:1.00
|
NE2
|
B:HIS67
|
2.0
|
13.3
|
1.0
|
SG
|
B:CYS174
|
2.2
|
15.6
|
1.0
|
N1
|
B:PYZ378
|
2.2
|
16.0
|
1.0
|
SG
|
B:CYS46
|
2.3
|
16.5
|
1.0
|
CD2
|
B:HIS67
|
3.0
|
15.5
|
1.0
|
CE1
|
B:HIS67
|
3.1
|
13.7
|
1.0
|
N2
|
B:PYZ378
|
3.2
|
16.6
|
1.0
|
C5
|
B:PYZ378
|
3.2
|
17.2
|
1.0
|
C5N
|
B:NAJ377
|
3.2
|
11.9
|
1.0
|
CB
|
B:CYS174
|
3.3
|
13.5
|
1.0
|
CB
|
B:CYS46
|
3.3
|
15.5
|
1.0
|
C4N
|
B:NAJ377
|
3.6
|
12.2
|
1.0
|
C6N
|
B:NAJ377
|
4.0
|
12.0
|
1.0
|
OG
|
B:SER48
|
4.2
|
14.9
|
1.0
|
CG
|
B:HIS67
|
4.2
|
13.7
|
1.0
|
ND1
|
B:HIS67
|
4.2
|
13.7
|
1.0
|
CB
|
B:SER48
|
4.2
|
14.9
|
1.0
|
C4
|
B:PYZ378
|
4.3
|
16.4
|
1.0
|
C3
|
B:PYZ378
|
4.4
|
18.6
|
1.0
|
NH2
|
B:ARG369
|
4.5
|
17.9
|
1.0
|
CE2
|
B:PHE93
|
4.6
|
14.8
|
1.0
|
CA
|
B:CYS174
|
4.7
|
12.2
|
1.0
|
CZ
|
B:PHE93
|
4.8
|
13.6
|
1.0
|
CA
|
B:CYS46
|
4.8
|
16.4
|
1.0
|
OE2
|
B:GLU68
|
4.9
|
18.3
|
1.0
|
N
|
B:SER48
|
5.0
|
14.5
|
1.0
|
C
|
B:CYS174
|
5.0
|
13.0
|
1.0
|
|
Zinc binding site 4 out
of 4 in 1n92
Go back to
Zinc Binding Sites List in 1n92
Zinc binding site 4 out
of 4 in the Horse Liver Alcohol Dehydrogenase Complexed with Nad+ and 4- Iodopyrazole
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 Complexed with Nad+ and 4- Iodopyrazole within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn376
b:16.7
occ:1.00
|
SG
|
B:CYS100
|
2.3
|
16.2
|
1.0
|
SG
|
B:CYS103
|
2.3
|
14.9
|
1.0
|
SG
|
B:CYS111
|
2.3
|
15.1
|
1.0
|
SG
|
B:CYS97
|
2.3
|
17.3
|
1.0
|
CB
|
B:CYS111
|
3.3
|
15.3
|
1.0
|
CB
|
B:CYS100
|
3.4
|
16.4
|
1.0
|
CB
|
B:CYS97
|
3.4
|
16.1
|
1.0
|
CB
|
B:CYS103
|
3.5
|
15.8
|
1.0
|
N
|
B:CYS97
|
3.5
|
14.3
|
1.0
|
CA
|
B:CYS111
|
3.8
|
14.3
|
1.0
|
N
|
B:CYS100
|
3.9
|
19.2
|
1.0
|
CA
|
B:CYS97
|
3.9
|
15.7
|
1.0
|
N
|
B:LEU112
|
4.0
|
15.0
|
1.0
|
N
|
B:GLY98
|
4.0
|
17.5
|
1.0
|
N
|
B:CYS103
|
4.2
|
15.5
|
1.0
|
CA
|
B:CYS100
|
4.2
|
17.8
|
1.0
|
C
|
B:CYS111
|
4.3
|
13.8
|
1.0
|
C
|
B:CYS97
|
4.3
|
16.8
|
1.0
|
CA
|
B:CYS103
|
4.4
|
15.3
|
1.0
|
N
|
B:LYS99
|
4.5
|
18.8
|
1.0
|
C
|
B:GLN96
|
4.6
|
15.2
|
1.0
|
C
|
B:CYS100
|
4.8
|
17.1
|
1.0
|
N
|
B:LYS113
|
4.9
|
15.4
|
1.0
|
CG
|
B:LYS113
|
4.9
|
18.7
|
1.0
|
CA
|
B:GLN96
|
4.9
|
14.0
|
1.0
|
O
|
B:CYS100
|
4.9
|
17.2
|
1.0
|
O
|
B:HOH464
|
5.0
|
31.7
|
1.0
|
CA
|
B:GLY98
|
5.0
|
18.7
|
1.0
|
|
Reference:
J.K.Rubach,
B.V.Plapp.
Amino Acid Residues in the Nicotinamide Binding Site Contribute to Catalysis By Horse Liver Alcohol Dehydrogenase Biochemistry V. 42 2907 2003.
ISSN: ISSN 0006-2960
PubMed: 12627956
DOI: 10.1021/BI0272656
Page generated: Wed Oct 16 17:13:32 2024
|