1QAE
THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED MAGNESIUM-WATER CLUSTER
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 | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 251 |
| Chain | Residue |
| A | ASN119 |
| A | HOH252 |
| A | HOH253 |
| A | HOH254 |
| A | HOH255 |
| A | HOH256 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 251 |
| Chain | Residue |
| B | ASN119 |
| B | HOH252 |
| B | HOH253 |
| B | HOH254 |
| B | HOH255 |
| B | HOH256 |
| site_id | ASA |
| Number of Residues | 9 |
| Details | ACTIVE SITE REGION IN MONOMER A WITH CATALYTIC MAGNESIUM WATER CLUSTER |
| Chain | Residue |
| A | HIS89 |
| A | GLU127 |
| A | ASN119 |
| A | MG251 |
| A | HOH252 |
| A | HOH253 |
| A | HOH254 |
| A | HOH255 |
| A | HOH256 |
| site_id | ASB |
| Number of Residues | 9 |
| Details | ACTIVE SITE REGION IN MONOMER B WITH CATALYTIC MAGNESIUM WATER CLUSTER |
| Chain | Residue |
| B | HIS89 |
| B | GLU127 |
| B | ASN119 |
| B | MG251 |
| B | HOH252 |
| B | HOH253 |
| B | HOH254 |
| B | HOH255 |
| B | HOH256 |
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 | Annotated By Reference To The Literature 1smn |
| Chain | Residue | Details |
| A | ASN119 | |
| A | ARG87 | |
| A | HIS89 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1smn |
| 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 |
