Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003998 | molecular_function | acylphosphatase activity |
A | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 100 |
Chain | Residue |
A | PHE21 |
A | ARG23 |
A | LYS24 |
A | LYS68 |
A | CL102 |
A | HOH135 |
A | HOH165 |
A | HOH177 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 101 |
Chain | Residue |
A | LYS32 |
A | HIS60 |
A | TRP64 |
A | LYS68 |
A | HOH135 |
A | HOH165 |
A | GLU29 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CL A 102 |
Chain | Residue |
A | VAL17 |
A | GLN18 |
A | GLY19 |
A | VAL20 |
A | PHE21 |
A | PHE22 |
A | SO4100 |
A | HOH107 |
Functional Information from PROSITE/UniProt
site_id | PS00150 |
Number of Residues | 11 |
Details | ACYLPHOSPHATASE_1 Acylphosphatase signature 1. IfGkVQGVfFR |
Chain | Residue | Details |
A | ILE13-ARG23 | |
site_id | PS00151 |
Number of Residues | 17 |
Details | ACYLPHOSPHATASE_2 Acylphosphatase signature 2. GWVQNtdqGtVqgqlqG |
Chain | Residue | Details |
A | GLY37-GLY53 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS24 | |
A | THR42 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 9016712 |
Chain | Residue | Details |
A | ARG23 | |
A | ASN41 | |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 923 |
Chain | Residue | Details |
A | LYS24 | electrostatic stabiliser |
A | THR42 | modifies pKa |