1B65
Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0004177 | molecular_function | aminopeptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0004177 | molecular_function | aminopeptidase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| E | 0004177 | molecular_function | aminopeptidase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| F | 0004177 | molecular_function | aminopeptidase activity |
| F | 0016787 | molecular_function | hydrolase activity |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 10673442 |
| Chain | Residue | Details |
| A | ASN218 | |
| A | GLY289 | |
| A | TYR146 | |
| A | SER288 | |
| A | SER250 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 676 |
| Chain | Residue | Details |
| A | TYR146 | electrostatic stabiliser |
| A | ASN218 | electrostatic stabiliser |
| A | SER250 | proton acceptor, proton donor |
| A | SER288 | electrostatic stabiliser |
| A | GLY289 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 676 |
| Chain | Residue | Details |
| B | TYR146 | electrostatic stabiliser |
| B | ASN218 | electrostatic stabiliser |
| B | SER250 | proton acceptor, proton donor |
| B | SER288 | electrostatic stabiliser |
| B | GLY289 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 676 |
| Chain | Residue | Details |
| C | TYR146 | electrostatic stabiliser |
| C | ASN218 | electrostatic stabiliser |
| C | SER250 | proton acceptor, proton donor |
| C | SER288 | electrostatic stabiliser |
| C | GLY289 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 676 |
| Chain | Residue | Details |
| D | TYR146 | electrostatic stabiliser |
| D | ASN218 | electrostatic stabiliser |
| D | SER250 | proton acceptor, proton donor |
| D | SER288 | electrostatic stabiliser |
| D | GLY289 | electrostatic stabiliser |
| site_id | MCSA5 |
| Number of Residues | 5 |
| Details | M-CSA 676 |
| Chain | Residue | Details |
| E | TYR146 | electrostatic stabiliser |
| E | ASN218 | electrostatic stabiliser |
| E | SER250 | proton acceptor, proton donor |
| E | SER288 | electrostatic stabiliser |
| E | GLY289 | electrostatic stabiliser |
| site_id | MCSA6 |
| Number of Residues | 5 |
| Details | M-CSA 676 |
| Chain | Residue | Details |
| F | TYR146 | electrostatic stabiliser |
| F | ASN218 | electrostatic stabiliser |
| F | SER250 | proton acceptor, proton donor |
| F | SER288 | electrostatic stabiliser |
| F | GLY289 | electrostatic stabiliser |
