Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003998 | molecular_function | acylphosphatase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0003998 | molecular_function | acylphosphatase activity |
| B | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 201 |
| Chain | Residue |
| A | VAL24 |
| A | HOH306 |
| A | HOH425 |
| A | GLN25 |
| A | GLY26 |
| A | VAL27 |
| A | GLY28 |
| A | PHE29 |
| A | ARG30 |
| A | ASN48 |
| A | HOH303 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 201 |
| Chain | Residue |
| A | SER66 |
| A | LEU69 |
| A | PHE88 |
| A | HOH307 |
| B | SER66 |
| B | LEU69 |
| B | PHE88 |
| B | HOH304 |
| B | HOH325 |
| B | HOH362 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 202 |
| Chain | Residue |
| B | VAL24 |
| B | GLN25 |
| B | GLY26 |
| B | VAL27 |
| B | GLY28 |
| B | PHE29 |
| B | ARG30 |
| B | ASN48 |
| B | HOH322 |
| B | HOH384 |
Functional Information from PROSITE/UniProt
| site_id | PS00150 |
| Number of Residues | 11 |
| Details | ACYLPHOSPHATASE_1 Acylphosphatase signature 1. VyGlVQGVgFR |
| Chain | Residue | Details |
| A | VAL20-ARG30 | |
| site_id | PS00151 |
| Number of Residues | 17 |
| Details | ACYLPHOSPHATASE_2 Acylphosphatase signature 2. GYAKNlpdGsVevvaeG |
| Chain | Residue | Details |
| A | GLY44-GLY60 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 172 |
| Details | Domain: {"description":"Acylphosphatase-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00520","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"16287076","evidenceCode":"ECO:0000269"}]} |
