1AKO
EXONUCLEASE III FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0004527 | molecular_function | exonuclease activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006281 | biological_process | DNA repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008311 | molecular_function | double-stranded DNA 3'-5' DNA exonuclease activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | MG1 |
| Number of Residues | 1 |
| Details | MG BINDING SITE. |
| Chain | Residue |
| A | GLU34 |
Functional Information from PROSITE/UniProt
| site_id | PS00726 |
| Number of Residues | 10 |
| Details | AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDVIGLQETK |
| Chain | Residue | Details |
| A | PRO27-LYS36 |
| site_id | PS00727 |
| Number of Residues | 17 |
| Details | AP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DTFRHanpqtadrFSWF |
| Chain | Residue | Details |
| A | ASP197-PHE213 |
| site_id | PS00728 |
| Number of Residues | 12 |
| Details | AP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NrGlRIDLlLaS |
| Chain | Residue | Details |
| A | ASN223-SER234 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Interaction with DNA substrate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 8092679 |
| Chain | Residue | Details |
| A | HIS259 | |
| A | ASP229 | |
| A | ASN7 | |
| A | ASP151 | |
| A | ASN153 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 160 |
| Chain | Residue | Details |
| A | ASN7 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | GLU34 | metal ligand |
| A | ASP151 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | ASN153 | activator, electrostatic stabiliser, hydrogen bond donor, metal ligand |
| A | ASP229 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | ASP258 | metal ligand |
| A | HIS259 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
