4DI8
CRYSTAL STRUCTURE OF THE D248A mutant of 2-PYRONE-4,6-DICARBOXYLIC ACID HYDROLASE FROM SPHINGOMONAS PAUCIMOBILIS complexed with substrate at pH 8.5
Replaces: 4D95Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| A | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| A | 0046274 | biological_process | lignin catabolic process |
| A | 0047554 | molecular_function | 2-pyrone-4,6-dicarboxylate lactonase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019439 | biological_process | obsolete aromatic compound catabolic process |
| B | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| B | 0046274 | biological_process | lignin catabolic process |
| B | 0047554 | molecular_function | 2-pyrone-4,6-dicarboxylate lactonase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 0GZ A 401 |
| Chain | Residue |
| A | HIS31 |
| A | HIS180 |
| A | ARG183 |
| A | ARG217 |
| A | ASN253 |
| A | ACT402 |
| A | HIS33 |
| A | TYR49 |
| A | ALA76 |
| A | SER77 |
| A | ARG124 |
| A | ARG130 |
| A | LEU131 |
| A | TYR156 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT A 402 |
| Chain | Residue |
| A | ARG130 |
| A | ARG183 |
| A | ARG217 |
| A | ASN253 |
| A | 0GZ401 |
| A | 0GY403 |
| A | HOH651 |
| A | HOH705 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 0GY A 403 |
| Chain | Residue |
| A | HIS31 |
| A | HIS33 |
| A | TYR49 |
| A | ALA76 |
| A | SER77 |
| A | ARG124 |
| A | ARG130 |
| A | LEU131 |
| A | TYR156 |
| A | HIS180 |
| A | ARG183 |
| A | ARG217 |
| A | PRO252 |
| A | ASN253 |
| A | ACT402 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 0GZ B 401 |
| Chain | Residue |
| B | HIS31 |
| B | HIS33 |
| B | TYR49 |
| B | SER77 |
| B | ARG124 |
| B | ARG130 |
| B | LEU131 |
| B | TYR156 |
| B | HIS180 |
| B | ARG183 |
| B | ARG217 |
| B | PRO252 |
| B | ASN253 |
| B | ACT402 |
| B | HOH698 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT B 402 |
| Chain | Residue |
| B | ARG130 |
| B | ARG183 |
| B | ARG217 |
| B | ASN253 |
| B | 0GY405 |
| B | HOH735 |
| B | HOH826 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 403 |
| Chain | Residue |
| B | HOH591 |
| B | HOH688 |
| B | HOH701 |
| B | HOH741 |
| B | HOH759 |
| B | HOH783 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 404 |
| Chain | Residue |
| B | HOH630 |
| B | HOH674 |
| B | HOH719 |
| B | HOH737 |
| B | HOH781 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 0GY B 405 |
| Chain | Residue |
| B | HIS31 |
| B | HIS33 |
| B | TYR49 |
| B | ALA76 |
| B | SER77 |
| B | ARG124 |
| B | ARG130 |
| B | LEU131 |
| B | TYR156 |
| B | HIS180 |
| B | ARG183 |
| B | ARG217 |
| B | PRO252 |
| B | ASN253 |
| B | ACT402 |
| B | HOH698 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:22475079 |
| Chain | Residue | Details |
| A | ALA248 | |
| B | ALA248 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22475079 |
| Chain | Residue | Details |
| B | HIS180 | |
| B | ASN253 | |
| A | TYR156 | |
| A | HIS180 | |
| A | ASN253 | |
| B | HIS31 | |
| B | TYR49 | |
| B | SER77 | |
| B | ARG124 | |
| B | ARG130 | |
| B | TYR156 | |
| A | HIS31 | |
| A | TYR49 | |
| A | SER77 | |
| A | ARG124 | |
| A | ARG130 |
