Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004518 | molecular_function | nuclease activity |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004518 | molecular_function | nuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE THP A 201 |
| Chain | Residue |
| A | ARG35 |
| A | TYR113 |
| A | TYR115 |
| A | CA202 |
| A | HOH301 |
| A | HOH310 |
| A | HOH330 |
| A | HOH337 |
| A | HOH340 |
| A | LEU36 |
| A | ASP40 |
| A | LYS71 |
| A | ASP83 |
| A | LYS84 |
| A | TYR85 |
| A | ARG87 |
| A | LEU89 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 202 |
| Chain | Residue |
| A | ASP21 |
| A | ASP40 |
| A | THR41 |
| A | THP201 |
| A | HOH320 |
| A | HOH330 |
| A | HOH331 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 203 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE THP B 201 |
| Chain | Residue |
| B | ARG35 |
| B | LEU36 |
| B | ASP40 |
| B | LYS71 |
| B | ASP83 |
| B | LYS84 |
| B | TYR85 |
| B | ARG87 |
| B | LEU89 |
| B | TYR113 |
| B | TYR115 |
| B | CA202 |
| B | HOH301 |
| B | HOH310 |
| B | HOH311 |
| B | HOH344 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 202 |
| Chain | Residue |
| B | ASP21 |
| B | ASP40 |
| B | THR41 |
| B | THP201 |
| B | HOH311 |
| B | HOH322 |
| B | HOH325 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PO4 B 203 |
Functional Information from PROSITE/UniProt
| site_id | PS01123 |
| Number of Residues | 25 |
| Details | TNASE_1 Thermonuclease family signature 1. DGDTMkLmykgqpmtf.RLllVDtPE |
| 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 | 32 |
| 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 | 6 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"288045","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| 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 | THR41 | 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 |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 165 |
| Chain | Residue | Details |
| B | ASP21 | metal ligand |
| B | ARG35 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP40 | metal ligand |
| B | THR41 | metal ligand |
| B | GLU43 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG87 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
