1EI6
CRYSTAL STRUCTURE OF PHOSPHONOACETATE HYDROLASE COMPLEXED WITH PHOSPHONOFORMATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019636 | biological_process | phosphonoacetate metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047400 | molecular_function | phosphonoacetate hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019636 | biological_process | phosphonoacetate metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047400 | molecular_function | phosphonoacetate hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019636 | biological_process | phosphonoacetate metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0047400 | molecular_function | phosphonoacetate hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019636 | biological_process | phosphonoacetate metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0047400 | molecular_function | phosphonoacetate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 408 |
| Chain | Residue |
| A | ASP25 |
| A | THR64 |
| A | ASP202 |
| A | ASP241 |
| A | HIS242 |
| A | PPF410 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 409 |
| Chain | Residue |
| A | PPF410 |
| A | ASP202 |
| A | HIS206 |
| A | HIS368 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 408 |
| Chain | Residue |
| B | ASP25 |
| B | THR64 |
| B | ASP241 |
| B | HIS242 |
| B | TLA411 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 409 |
| Chain | Residue |
| B | ASP202 |
| B | HIS206 |
| B | HIS368 |
| B | TLA411 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 408 |
| Chain | Residue |
| C | ASP25 |
| C | THR64 |
| C | ASP241 |
| C | HIS242 |
| C | PPF413 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 409 |
| Chain | Residue |
| C | ASP202 |
| C | HIS206 |
| C | HIS368 |
| C | PPF413 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 408 |
| Chain | Residue |
| D | ASP25 |
| D | THR64 |
| D | ASP241 |
| D | HIS242 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 409 |
| Chain | Residue |
| D | ASP202 |
| D | HIS206 |
| D | HIS368 |
| D | PPF412 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TLA B 411 |
| Chain | Residue |
| B | PHE63 |
| B | THR64 |
| B | ASN85 |
| B | ASP202 |
| B | HIS206 |
| B | ILE278 |
| B | HIS285 |
| B | HIS286 |
| B | HIS368 |
| B | ZN408 |
| B | ZN409 |
| B | HOH590 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PPF A 410 |
| Chain | Residue |
| A | THR64 |
| A | ASP202 |
| A | HIS206 |
| A | HIS242 |
| A | ILE278 |
| A | HIS368 |
| A | ZN408 |
| A | ZN409 |
| A | HOH470 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PPF D 412 |
| Chain | Residue |
| D | THR64 |
| D | ASP202 |
| D | HIS206 |
| D | ILE278 |
| D | HIS285 |
| D | HIS286 |
| D | HIS368 |
| D | ZN409 |
| D | HOH703 |
| D | HOH879 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PPF C 413 |
| Chain | Residue |
| C | ASP25 |
| C | PHE63 |
| C | THR64 |
| C | ASP202 |
| C | HIS206 |
| C | HIS242 |
| C | ILE278 |
| C | HIS368 |
| C | ZN408 |
| C | ZN409 |
| C | HOH808 |
| C | HOH845 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2000","submissionDatabase":"PDB data bank","title":"Crystal structure of phosphonoacetate hydrolase complexed with phosphonoformate.","authors":["Holden H.M.","Benning M.M.","Dunaway-Mariano D.","Kim A.D."]}}]} |
| Chain | Residue | Details |
