3G91
1.2 Angstrom structure of the exonuclease III homologue Mth0212
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0006281 | biological_process | DNA repair |
| A | 0006284 | biological_process | base-excision repair |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| A | 0008311 | molecular_function | double-stranded DNA 3'-5' DNA exonuclease activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2001 |
| Chain | Residue |
| A | ASN10 |
| A | HOH7054 |
| A | HOH7110 |
| A | HOH7214 |
| A | HOH7216 |
| A | HOH7257 |
| A | GLU38 |
| A | TYR111 |
| A | ASN114 |
| A | ASP151 |
| A | ASN153 |
| A | HIS248 |
| A | MG3001 |
| A | HOH7020 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 3001 |
| Chain | Residue |
| A | GLU38 |
| A | PO42001 |
| A | HOH7020 |
| A | HOH7054 |
| A | HOH7110 |
| A | HOH7183 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 3011 |
| Chain | Residue |
| A | ARG48 |
| A | ARG51 |
| A | ARG140 |
| A | ASP141 |
| A | HOH7018 |
| A | HOH7161 |
| A | HOH7320 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEG A 3021 |
| Chain | Residue |
| A | ARG51 |
| A | HIS52 |
| A | TYR56 |
| A | ARG57 |
| A | SER58 |
| A | PHE59 |
| A | HOH7071 |
| A | HOH7218 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 A 3022 |
| Chain | Residue |
| A | VAL3 |
| A | ASP32 |
| A | GLU254 |
Functional Information from PROSITE/UniProt
| site_id | PS00726 |
| Number of Residues | 10 |
| Details | AP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQEIK |
| Chain | Residue | Details |
| A | PRO31-LYS40 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"20434457","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20434457","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2012","submissionDatabase":"PDB data bank","title":"Crystal structure of DNA uridine endonuclease Mth212.","authors":["Tabata N.","Shida T.","Arai R."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20434457","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
