1SMN
IDENTIFICATION OF THE SERRATIA ENDONUCLEASE DIMER: STRUCTURAL BASIS AND IMPLICATIONS FOR CATALYSIS
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 | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | ASA |
| Number of Residues | 2 |
| Details | PUTATIVE ACTIVE SITE REGION IN MONOMER A |
| Chain | Residue |
| A | HIS89 |
| A | GLU127 |
| site_id | ASB |
| Number of Residues | 2 |
| Details | PUTATIVE ACTIVE SITE REGION IN MONOMER B |
| Chain | Residue |
| B | HIS89 |
| B | GLU127 |
| site_id | INT |
| Number of Residues | 37 |
| Details | RESIDUES IN THE PHYSIOLOGICAL DIMER INTERFACE |
| Chain | Residue |
| A | VAL182 |
| A | ASN183 |
| A | HIS184 |
| A | ASP225 |
| A | SER229 |
| A | LYS233 |
| A | VAL236 |
| A | GLU239 |
| A | LEU240 |
| A | ASN245 |
| B | ARG136 |
| B | ASP138 |
| B | ASN178 |
| B | PRO180 |
| B | ALA181 |
| B | VAL182 |
| B | ASN183 |
| B | HIS184 |
| B | ASP225 |
| B | SER229 |
| B | LYS233 |
| B | VAL236 |
| B | GLU239 |
| B | LEU240 |
| B | ASN245 |
| B | HOH248 |
| A | HOH248 |
| B | HOH260 |
| B | HOH294 |
| B | HOH296 |
| A | HOH309 |
| A | HOH311 |
| A | ARG136 |
| A | ASP138 |
| A | ASN178 |
| A | PRO180 |
| A | ALA181 |
Functional Information from PROSITE/UniProt
| site_id | PS01070 |
| Number of Residues | 9 |
| Details | NUCLEASE_NON_SPEC DNA/RNA non-specific endonucleases active site. DRGHQaplA |
| Chain | Residue | Details |
| A | ASP86-ALA94 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10047","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8078761","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10771425, 7664065, 9257723 |
| Chain | Residue | Details |
| A | ASN119 | |
| A | ARG87 | |
| A | HIS89 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10771425, 7664065, 9257723 |
| Chain | Residue | Details |
| B | ASN119 | |
| B | ARG87 | |
| B | HIS89 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 42 |
| Chain | Residue | Details |
| A | ARG57 | electrostatic stabiliser |
| A | HIS89 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASN110 | electrostatic stabiliser, increase acidity, increase basicity |
| A | ASN119 | activator, hydrogen bond acceptor, hydrogen bond donor, metal ligand |
| A | GLU127 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 42 |
| Chain | Residue | Details |
| B | ARG57 | electrostatic stabiliser |
| B | HIS89 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN110 | electrostatic stabiliser, increase acidity, increase basicity |
| B | ASN119 | activator, hydrogen bond acceptor, hydrogen bond donor, metal ligand |
| B | GLU127 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |
