3V1M
Crystal Structure of the S112A/H265Q mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400, after exposure to its substrate HOPDA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0009056 | biological_process | catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016823 | molecular_function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances |
| A | 0018771 | molecular_function | 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity |
| A | 0018774 | molecular_function | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity |
| A | 0046464 | biological_process | acylglycerol catabolic process |
| A | 0047372 | molecular_function | monoacylglycerol lipase activity |
| A | 0070980 | biological_process | biphenyl catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MLI A 287 |
| Chain | Residue |
| A | GLU34 |
| A | HOH379 |
| A | HOH391 |
| A | HOH392 |
| A | THR35 |
| A | ARG65 |
| A | ILE103 |
| A | ASP104 |
| A | ARG105 |
| A | SER180 |
| A | ILE182 |
| A | HOH316 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HPK A 288 |
| Chain | Residue |
| A | GLY41 |
| A | GLY42 |
| A | GLY43 |
| A | ALA46 |
| A | ALA112 |
| A | MET113 |
| A | ILE153 |
| A | PHE175 |
| A | ARG190 |
| A | VAL240 |
| A | TRP266 |
| A | HOH374 |
| A | HOH399 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
