1AK0
P1 NUCLEASE IN COMPLEX WITH A SUBSTRATE ANALOG
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0006308 | biological_process | DNA catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Region: {"description":"Substrate binding","evidences":[{"source":"PubMed","id":"9726413","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AK0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9C9G4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 17 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9726413","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AK0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P24021","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"9726413","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AK0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9726413","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AK0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 9726413 |
| Chain | Residue | Details |
| A | ARG48 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 395 |
| Chain | Residue | Details |
| A | TRP1 | metal ligand |
| A | ASP153 | metal ligand |
| A | HIS6 | metal ligand |
| A | ASP45 | activator, metal ligand |
| A | ARG48 | electrostatic stabiliser |
| A | HIS60 | metal ligand |
| A | HIS116 | metal ligand |
| A | ASP120 | metal ligand |
| A | HIS126 | metal ligand |
| A | HIS149 | metal ligand |
