1AM5
THE CRYSTAL STRUCTURE AND PROPOSED AMINO ACID SEQUENCE OF A PEPSIN FROM ATLANTIC COD (GADUS MORHUA)
Functional Information from GO Data
Functional Information from PDB Data
| site_id | CAT |
| Number of Residues | 2 |
| Details | THE CATALYTIC ASPARTIC RESIDUES, ASP 32 AND ASP 215, ARE CONNECTED THROUGH A NETWORK OF HYDROGEN BONDS. |
| Chain | Residue |
| A | ASP32 |
| A | ASP215 |
Functional Information from PROSITE/UniProt
| site_id | PS00141 |
| Number of Residues | 12 |
| Details | ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIFDTGSSNLWV |
| Chain | Residue | Details |
| A | VAL29-VAL40 | |
| A | ALA212-ALA223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 307 |
| Details | Domain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 23 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 396 |
| Chain | Residue | Details |
| A | ASP32 | proton acceptor, proton donor |
| A | SER35 | electrostatic stabiliser, modifies pKa |
| A | ASN37 | electrostatic stabiliser, modifies pKa |
| A | TRP39 | electrostatic stabiliser, modifies pKa |
| A | TYR75 | electrostatic stabiliser, modifies pKa |
| A | ASP215 | proton acceptor, proton donor |
| A | THR218 | electrostatic stabiliser, modifies pKa |
