Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004518 | molecular_function | nuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE THP A 201 |
| Chain | Residue |
| A | ARG35 |
| A | HOH308 |
| A | HOH310 |
| A | HOH311 |
| A | HOH331 |
| A | HOH336 |
| A | HOH338 |
| A | HOH342 |
| A | HOH347 |
| A | HOH350 |
| A | HOH357 |
| A | LYS84 |
| A | HOH365 |
| A | TYR85 |
| A | ARG87 |
| A | LEU89 |
| A | TYR113 |
| A | TYR115 |
| A | LYS127 |
| A | HOH305 |
Functional Information from PROSITE/UniProt
| site_id | PS01123 |
| Number of Residues | 25 |
| Details | TNASE_1 Thermonuclease family signature 1. DGDTVkLmykgqpmvf.RLllVDiPE |
| Chain | Residue | Details |
| A | ASP19-GLU43 | |
| site_id | PS01284 |
| Number of Residues | 11 |
| Details | TNASE_2 Thermonuclease family signature 2. DKYGRgLAyIY |
| Chain | Residue | Details |
| A | ASP83-TYR93 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"288045","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 165 |
| Chain | Residue | Details |
| A | ASP21 | metal ligand |
| A | ARG35 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP40 | metal ligand |
| A | ILE41 | metal ligand |
| A | GLU43 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG87 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
