3V1K
Crystal Structure of the H265Q mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0009056 | biological_process | catabolic process |
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 |
B | 0003824 | molecular_function | catalytic activity |
B | 0009056 | biological_process | catabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016823 | molecular_function | hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances |
B | 0018771 | molecular_function | 2-hydroxy-6-oxonona-2,4-dienedioate hydrolase activity |
B | 0018774 | molecular_function | 2,6-dioxo-6-phenylhexa-3-enoate hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MLA A 287 |
Chain | Residue |
A | GLY41 |
A | TRP266 |
A | GLY43 |
A | ALA46 |
A | ASN51 |
A | ASN111 |
A | SER112 |
A | PHE175 |
A | ARG190 |
A | GLN265 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | GLN265 | |
B | GLN265 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY42 | |
B | SER180 | |
B | ARG190 | |
B | TRP266 | |
A | ASN51 | |
A | ASN111 | |
A | SER180 | |
A | ARG190 | |
A | TRP266 | |
B | GLY42 | |
B | ASN51 | |
B | ASN111 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | SER112 | |
B | SER112 |