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 | 6 |
| Details | binding site for residue CA A 201 |
| Chain | Residue |
| A | ASP19 |
| A | ASP21 |
| A | HOH350 |
| A | HOH354 |
| A | HOH365 |
| A | HOH378 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue THP A 202 |
| Chain | Residue |
| A | TYR85 |
| A | ARG87 |
| A | LEU89 |
| A | TYR113 |
| A | HOH310 |
| A | HOH315 |
| A | HOH350 |
| A | HOH359 |
| A | HOH363 |
| A | HOH364 |
| A | HOH365 |
| A | HOH366 |
| A | HOH385 |
| A | HOH405 |
| A | HOH419 |
| B | ARG105 |
| A | ARG35 |
| A | ASP40 |
| A | LYS84 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 201 |
| Chain | Residue |
| B | ASP19 |
| B | ASP21 |
| B | HOH312 |
| B | HOH344 |
| B | HOH353 |
| B | HOH360 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue THP B 202 |
| Chain | Residue |
| A | ARG105 |
| B | ALA1 |
| B | ARG35 |
| B | ASP40 |
| B | LYS84 |
| B | TYR85 |
| B | ARG87 |
| B | LEU89 |
| B | TYR113 |
| B | TYR115 |
| B | HOH306 |
| B | HOH307 |
| B | HOH312 |
| B | HOH315 |
| B | HOH344 |
| B | HOH365 |
| B | HOH366 |
| B | HOH377 |
| B | HOH392 |
Functional Information from PROSITE/UniProt
| site_id | PS01123 |
| Number of Residues | 25 |
| Details | TNASE_1 Thermonuclease family signature 1. DGDTVkLmykgqpmtf.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 |
