2OG1
Crystal Structure of BphD, a C-C hydrolase 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 | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 501 |
Chain | Residue |
B | GLY41 |
B | GLY43 |
B | ALA46 |
B | ASN51 |
B | PHE175 |
B | ARG190 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | ASN51 |
A | ASN111 |
A | ARG190 |
A | TRP266 |
A | HOH986 |
A | HOH987 |
A | HOH1021 |
A | GLY41 |
A | GLY43 |
A | ALA46 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | LYS14 |
A | ARG196 |
A | HOH927 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 504 |
Chain | Residue |
A | ILE103 |
A | ASP104 |
A | ARG105 |
A | HOH855 |
A | HOH985 |
A | HOH1017 |
B | LYS202 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 601 |
Chain | Residue |
A | TRP49 |
A | TYR53 |
A | GLU185 |
A | LEU186 |
A | HOH703 |
A | HOH785 |
A | HOH825 |
A | HOH924 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EOH A 701 |
Chain | Residue |
A | ASN16 |
A | HOH775 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EOH A 702 |
Chain | Residue |
A | ALA30 |
A | GLY31 |
A | HOH873 |
A | HOH1010 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EOH B 703 |
Chain | Residue |
B | GLU6 |
B | SER10 |
B | HIS26 |
B | ASN28 |
B | LYS76 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS265 | |
B | HIS265 |
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 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1azw |
Chain | Residue | Details |
A | ASP237 | |
A | HIS265 | |
A | SER112 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1azw |
Chain | Residue | Details |
B | ASP237 | |
B | HIS265 | |
B | SER112 |