4E3Y
X-ray structure of the Serratia marcescens endonuclease at 0.95 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
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 | 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 2601 |
Chain | Residue |
A | ASN1119 |
A | HOH2701 |
A | HOH2702 |
A | HOH2703 |
A | HOH2704 |
A | HOH2705 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 2602 |
Chain | Residue |
A | HOH2729 |
B | ASP2208 |
B | LYS2212 |
A | ALA1169 |
A | ASP1191 |
A | ARG1213 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PEG A 2603 |
Chain | Residue |
A | THR1035 |
A | LYS1037 |
A | LYS1162 |
A | ALA1163 |
A | HOH2781 |
A | HOH2782 |
A | HOH2979 |
A | HOH3023 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 2301 |
Chain | Residue |
B | ASN2119 |
B | HOH2401 |
B | HOH2402 |
B | HOH2403 |
B | HOH2404 |
B | HOH2405 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 B 2302 |
Chain | Residue |
A | ASN1020 |
B | GLY2054 |
B | ARG2057 |
B | ALA2094 |
B | HOH2475 |
B | HOH2592 |
B | HOH2593 |
B | HOH2630 |
B | HOH2684 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 B 2303 |
Chain | Residue |
A | ASN1020 |
B | ARG2057 |
B | ARG2087 |
B | HIS2089 |
B | ASN2119 |
B | HOH2401 |
B | HOH2402 |
B | HOH2572 |
B | HOH2712 |
B | HOH2735 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 2304 |
Chain | Residue |
B | THR2077 |
B | GLY2078 |
B | ARG2087 |
B | HOH2517 |
B | HOH2704 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 2305 |
Chain | Residue |
B | PRO2051 |
B | ARG2131 |
B | ILE2134 |
B | ASP2135 |
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 | ASP1086-ALA1094 |
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 | HIS1089 | |
B | HIS2089 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASN1119 | |
B | ASN2119 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 42 |
Chain | Residue | Details |
A | ARG1057 | electrostatic stabiliser |
A | HIS1089 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ASN1110 | electrostatic stabiliser, increase acidity, increase basicity |
A | ASN1119 | activator, hydrogen bond acceptor, hydrogen bond donor, metal ligand |
A | GLU1127 | 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 | ARG2057 | electrostatic stabiliser |
B | HIS2089 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ASN2110 | electrostatic stabiliser, increase acidity, increase basicity |
B | ASN2119 | activator, hydrogen bond acceptor, hydrogen bond donor, metal ligand |
B | GLU2127 | electrostatic stabiliser, hydrogen bond acceptor, metal ligand, proton acceptor, proton donor |