2PU7
Crystal Structure of S112A/H265A double mutant of a C-C hydrolase, BphD, from Burkholderia xenovorans LB400
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 287 |
| Chain | Residue |
| A | ARG105 |
| A | MLI288 |
| A | HOH361 |
| A | HOH362 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MLI A 288 |
| Chain | Residue |
| A | ARG105 |
| A | SER180 |
| A | NA287 |
| A | GLU34 |
| A | THR35 |
| A | ARG65 |
| A | ILE103 |
| A | ASP104 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MLI A 289 |
| Chain | Residue |
| A | GLY41 |
| A | GLY43 |
| A | ASN111 |
| A | ALA112 |
| A | PHE175 |
| A | ARG190 |
| A | ALA265 |
| A | TRP266 |
| A | HOH329 |
| A | HOH355 |
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 |
