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 | 0006281 | biological_process | DNA repair |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0006281 | biological_process | DNA repair |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 401 |
| Chain | Residue |
| A | ASP70 |
| A | GLU96 |
| A | HOH504 |
| A | HOH516 |
| A | HOH527 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue MN A 402 |
| Chain | Residue |
| A | HOH604 |
| A | HOH631 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue MN A 403 |
| Chain | Residue |
| P | DG13 |
| A | GLY225 |
| A | ASN229 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | ASP189 |
| A | GLY239 |
| A | PHE240 |
| A | HOH509 |
| A | HOH539 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | LEU44 |
| A | TYR45 |
| A | ASN277 |
| A | HOH537 |
| A | HOH540 |
| A | HOH613 |
| A | HOH669 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | LYS63 |
| A | GLU86 |
| A | GLU87 |
| A | LEU179 |
| A | HOH510 |
| A | HOH581 |
| A | HOH612 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | THR268 |
| A | TYR269 |
| A | ASP308 |
| P | DC12 |
| V | DG12 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 408 |
| Chain | Residue |
| A | GLU101 |
| A | TYR118 |
| A | TRP119 |
| A | HOH566 |
| B | HIS116 |
| B | ARG136 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue MN B 401 |
| Chain | Residue |
| B | LYS228 |
| B | ASN229 |
| B | HOH504 |
| B | HOH591 |
| B | HOH624 |
| B | HOH637 |
| V | DG1 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | ASP189 |
| B | PHE240 |
| B | HOH539 |
| B | HOH549 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue MN P 101 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue MN P 102 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue MN P 103 |
Functional Information from PROSITE/UniProt
| site_id | PS00726 |
| Number of Residues | 10 |
| Details | AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK |
| Chain | Residue | Details |
| A | PRO89-LYS98 | |
| site_id | PS00727 |
| Number of Residues | 17 |
| Details | AP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW |
| Chain | Residue | Details |
| A | ASP251-TRP267 | |
| site_id | PS00728 |
| Number of Residues | 12 |
| Details | AP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS |
| Chain | Residue | Details |
| A | ASN277-SER288 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | Region: {"description":"Mitochondrial targeting sequence (MTS)"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Motif: {"description":"Nuclear export signal (NES)"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"15380100","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9351835","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BIX","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00764","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00764","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8932375","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"21762700","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9804799","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Site: {"description":"Interaction with DNA substrate"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"PubMed","id":"17403694","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by CDK5","evidences":[{"source":"UniProtKB","id":"P28352","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"17403694","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 510 |
| Chain | Residue | Details |
| A | ASP70 | metal ligand |
| A | GLU96 | metal ligand |
| A | TYR171 | electrostatic stabiliser, metal ligand |
| A | ASP210 | increase nucleophilicity, metal ligand, proton acceptor |
| A | ASN212 | |
| A | ASP283 | electrostatic stabiliser |
| A | ASP308 | metal ligand |
| A | HIS309 | electrostatic stabiliser, metal ligand |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 510 |
| Chain | Residue | Details |
| B | ASP70 | metal ligand |
| B | GLU96 | metal ligand |
| B | TYR171 | electrostatic stabiliser, metal ligand |
| B | ASP210 | increase nucleophilicity, metal ligand, proton acceptor |
| B | ASN212 | |
| B | ASP283 | electrostatic stabiliser |
| B | ASP308 | metal ligand |
| B | HIS309 | electrostatic stabiliser, metal ligand |
