1O8U
The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016823 | molecular_function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016823 | molecular_function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016823 | molecular_function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016823 | molecular_function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances |
E | 0016787 | molecular_function | hydrolase activity |
E | 0016823 | molecular_function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances |
F | 0016787 | molecular_function | hydrolase activity |
F | 0016823 | molecular_function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE NA A1253 |
Chain | Residue |
A | HOH2130 |
A | HOH2131 |
B | ASP186 |
B | HOH2123 |
B | HOH2126 |
C | ASP186 |
C | HOH2120 |
C | HOH2122 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA D1253 |
Chain | Residue |
E | ASP186 |
E | HOH2129 |
E | HOH2130 |
F | HOH2113 |
F | HOH2115 |
F | HOH2116 |
D | HOH2109 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | GLU124 | |
B | GLU124 | |
C | GLU124 | |
D | GLU124 | |
E | GLU124 | |
F | GLU124 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15138275 |
Chain | Residue | Details |
A | TRP40 | |
C | HIS145 | |
C | ASP154 | |
C | GLU244 | |
D | TRP40 | |
D | HIS145 | |
D | ASP154 | |
D | GLU244 | |
E | TRP40 | |
E | HIS145 | |
E | ASP154 | |
A | HIS145 | |
E | GLU244 | |
F | TRP40 | |
F | HIS145 | |
F | ASP154 | |
F | GLU244 | |
A | ASP154 | |
A | GLU244 | |
B | TRP40 | |
B | HIS145 | |
B | ASP154 | |
B | GLU244 | |
C | TRP40 |