1SMN
IDENTIFICATION OF THE SERRATIA ENDONUCLEASE DIMER: STRUCTURAL BASIS AND IMPLICATIONS FOR CATALYSIS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000014 | molecular_function | single-stranded DNA endodeoxyribonuclease activity |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004518 | molecular_function | nuclease activity |
A | 0004519 | molecular_function | endonuclease activity |
A | 0004521 | molecular_function | RNA endonuclease activity |
A | 0005576 | cellular_component | extracellular region |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000014 | molecular_function | single-stranded DNA endodeoxyribonuclease activity |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0004518 | molecular_function | nuclease activity |
B | 0004519 | molecular_function | endonuclease activity |
B | 0004521 | molecular_function | RNA 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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10047, ECO:0000269|PubMed:8078761 |
Chain | Residue | Details |
A | HIS89 | |
B | HIS89 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN119 | |
B | ASN119 |
Catalytic Information from CSA
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 |