3G0R
Complex of Mth0212 and an 8bp dsDNA with distorted ends
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 |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0006281 | biological_process | DNA repair |
| B | 0006284 | biological_process | base-excision repair |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| B | 0008311 | molecular_function | double-stranded DNA 3'-5' DNA exonuclease activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 266 |
| Chain | Residue |
| A | ASP130 |
| A | TRP180 |
| A | HOH313 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 267 |
| Chain | Residue |
| A | PHE102 |
| A | HOH309 |
| A | LEU4 |
| A | ASP32 |
| A | ILE33 |
| A | THR75 |
| A | LYS76 |
| A | VAL77 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 268 |
| Chain | Residue |
| A | ASP191 |
| A | THR192 |
| A | PHE193 |
| A | ARG220 |
| A | ASP222 |
| A | TYR223 |
| A | PHE224 |
| A | TRP238 |
| A | ILE251 |
| A | HOH326 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 269 |
| Chain | Residue |
| A | THR61 |
| A | PRO62 |
| A | GLU84 |
| A | PHE91 |
| A | ASP92 |
| A | THR93 |
| A | GLU94 |
| A | GLY95 |
| A | ARG96 |
| A | ILE97 |
| A | PG4275 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 270 |
| Chain | Residue |
| A | ILE185 |
| A | VAL190 |
| A | ASP191 |
| A | ARG194 |
| A | MET195 |
| A | HOH282 |
| A | HOH303 |
| A | HOH415 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 271 |
| Chain | Residue |
| A | LYS20 |
| A | TYR208 |
| A | GLY245 |
| A | SER246 |
| A | HOH387 |
| A | HOH423 |
| K | DT4 |
| K | DG5 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 272 |
| Chain | Residue |
| A | HIS156 |
| A | ARG157 |
| A | ARG178 |
| A | ASP182 |
| A | HOH407 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 273 |
| Chain | Residue |
| A | GLU29 |
| A | TRP238 |
| A | LEU240 |
| A | HOH302 |
| A | HOH353 |
| A | HOH418 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 274 |
| Chain | Residue |
| A | ASN137 |
| A | ARG140 |
| A | ASP141 |
| A | ASN187 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 A 275 |
| Chain | Residue |
| A | ALA42 |
| A | GLU44 |
| A | GLN45 |
| A | PRO62 |
| A | ALA63 |
| A | GLU64 |
| A | GOL269 |
| A | HOH322 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 A 276 |
| Chain | Residue |
| A | ARG51 |
| A | HIS52 |
| A | GLY55 |
| A | TYR56 |
| A | ARG57 |
| A | SER58 |
| A | HOH404 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 A 277 |
| Chain | Residue |
| A | TRP9 |
| A | VAL17 |
| A | LYS20 |
| A | TRP25 |
| A | ASP242 |
| A | MET244 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 266 |
| Chain | Residue |
| B | PHE193 |
| B | ARG220 |
| B | ASP222 |
| B | PHE224 |
| B | SER237 |
| B | TRP238 |
| B | ILE239 |
| B | ILE251 |
| B | GLY252 |
| B | HOH300 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 267 |
| Chain | Residue |
| B | ASP130 |
| B | TRP180 |
| B | HOH344 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 268 |
| Chain | Residue |
| B | LYS76 |
| B | GLY55 |
| B | ARG57 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA G 14 |
| Chain | Residue |
| G | DC5 |
| G | DG6 |
| G | HOH16 |
| K | DG5 |
| K | DU6 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA G 15 |
| Chain | Residue |
| G | DG4 |
| G | DC5 |
| K | DU6 |
| K | DG7 |
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 | 2 |
| 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 | 4 |
| 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 | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20434457","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






