1ZO8
X-ray Structure of the haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (S)-para-nitrostyrene oxide, with a water molecule in the halide-binding site
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
I | 0016491 | molecular_function | oxidoreductase activity |
I | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
M | 0016491 | molecular_function | oxidoreductase activity |
M | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
N | 0016491 | molecular_function | oxidoreductase activity |
N | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
O | 0016491 | molecular_function | oxidoreductase activity |
O | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
P | 0016491 | molecular_function | oxidoreductase activity |
P | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SNO A 5002 |
Chain | Residue |
A | PRO84 |
A | HOH5003 |
C | TRP249 |
A | PHE86 |
A | SER132 |
A | TRP139 |
A | TYR145 |
A | PRO175 |
A | ASN176 |
A | PHE186 |
A | TYR187 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SNO B 5001 |
Chain | Residue |
B | PHE12 |
B | PRO84 |
B | PHE86 |
B | SER132 |
B | TRP139 |
B | TYR145 |
B | PRO175 |
B | ASN176 |
B | PHE186 |
B | TYR187 |
B | HOH5002 |
D | TRP249 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SNO C 5003 |
Chain | Residue |
A | TRP249 |
C | PRO84 |
C | PHE86 |
C | SER132 |
C | TRP139 |
C | TYR145 |
C | PRO175 |
C | ASN176 |
C | PHE186 |
C | TYR187 |
C | HOH5004 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SNO D 5004 |
Chain | Residue |
B | TRP249 |
D | PRO84 |
D | PHE86 |
D | SER132 |
D | TRP139 |
D | TYR145 |
D | PRO175 |
D | ASN176 |
D | PHE186 |
D | TYR187 |
D | HOH5005 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SNO E 5006 |
Chain | Residue |
E | PRO84 |
E | PHE86 |
E | SER132 |
E | TRP139 |
E | TYR145 |
E | PRO175 |
E | ASN176 |
E | PHE186 |
E | HOH5007 |
G | TRP249 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SNO F 5005 |
Chain | Residue |
F | PHE12 |
F | PRO84 |
F | PHE86 |
F | SER132 |
F | TRP139 |
F | TYR145 |
F | PRO175 |
F | ASN176 |
F | PHE186 |
F | TYR187 |
F | HOH5006 |
H | TRP249 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SNO G 5007 |
Chain | Residue |
E | TRP249 |
G | PHE12 |
G | PRO84 |
G | PHE86 |
G | SER132 |
G | TRP139 |
G | TYR145 |
G | PRO175 |
G | ASN176 |
G | PHE186 |
G | TYR187 |
G | HOH5008 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SNO H 5008 |
Chain | Residue |
F | TRP249 |
H | PRO84 |
H | PHE86 |
H | SER132 |
H | TRP139 |
H | TYR145 |
H | PRO175 |
H | ASN176 |
H | PHE186 |
H | TYR187 |
H | HOH5009 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SNO I 5010 |
Chain | Residue |
I | TYR187 |
I | HOH5011 |
K | TRP249 |
I | PHE12 |
I | PRO84 |
I | PHE86 |
I | SER132 |
I | TRP139 |
I | TYR145 |
I | PRO175 |
I | ASN176 |
I | PHE186 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SNO J 5009 |
Chain | Residue |
J | PRO84 |
J | PHE86 |
J | SER132 |
J | TRP139 |
J | TYR145 |
J | PRO175 |
J | PHE186 |
J | TYR187 |
J | HOH5010 |
L | TRP249 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SNO K 5011 |
Chain | Residue |
I | TRP249 |
K | PRO84 |
K | PHE86 |
K | SER132 |
K | TRP139 |
K | TYR145 |
K | PRO175 |
K | ASN176 |
K | PHE186 |
K | HOH5012 |
site_id | BC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SNO L 5012 |
Chain | Residue |
J | TRP249 |
L | PHE12 |
L | PRO84 |
L | PHE86 |
L | SER132 |
L | TRP139 |
L | TYR145 |
L | PRO175 |
L | ASN176 |
L | PHE186 |
L | HOH5013 |
site_id | BC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SNO M 5014 |
Chain | Residue |
M | PHE12 |
M | PRO84 |
M | PHE86 |
M | SER132 |
M | TRP139 |
M | TYR145 |
M | PRO175 |
M | ASN176 |
M | PHE186 |
M | TYR187 |
M | TRP249 |
M | HOH5015 |
site_id | BC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SNO N 5013 |
Chain | Residue |
N | PHE12 |
N | PRO84 |
N | PHE86 |
N | SER132 |
N | TRP139 |
N | TYR145 |
N | PRO175 |
N | ASN176 |
N | PHE186 |
N | TYR187 |
N | TRP249 |
N | HOH5014 |
site_id | BC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SNO O 5016 |
Chain | Residue |
O | PHE12 |
O | PRO84 |
O | PHE86 |
O | SER132 |
O | TRP139 |
O | TYR145 |
O | PRO175 |
O | ASN176 |
O | PHE186 |
O | TYR187 |
O | TRP249 |
O | HOH5017 |
site_id | BC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SNO P 5015 |
Chain | Residue |
P | PRO84 |
P | PHE86 |
P | SER132 |
P | TRP139 |
P | TYR145 |
P | PRO175 |
P | ASN176 |
P | PHE186 |
P | TRP249 |
P | HOH5016 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
A | TYR145 | |
A | ARG149 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
J | TYR145 | |
J | ARG149 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
K | TYR145 | |
K | ARG149 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
L | TYR145 | |
L | ARG149 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
M | TYR145 | |
M | ARG149 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
N | TYR145 | |
N | ARG149 |
site_id | CSA15 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
O | TYR145 | |
O | ARG149 |
site_id | CSA16 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
P | TYR145 | |
P | ARG149 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
B | TYR145 | |
B | ARG149 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
C | TYR145 | |
C | ARG149 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
D | TYR145 | |
D | ARG149 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
E | TYR145 | |
E | ARG149 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
F | TYR145 | |
F | ARG149 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
G | TYR145 | |
G | ARG149 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
H | TYR145 | |
H | ARG149 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1gz6 |
Chain | Residue | Details |
I | TYR145 | |
I | ARG149 |