3G00
Mth0212 in complex with a 9bp blunt end dsDNA at 1.7 Angstrom
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 | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 266 |
| Chain | Residue |
| A | PHE59 |
| A | PRO79 |
| A | HOH361 |
| A | HOH450 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 267 |
| Chain | Residue |
| A | GLU44 |
| A | LEU46 |
| A | PRO47 |
| A | HOH396 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 268 |
| Chain | Residue |
| A | TYR68 |
| A | GLU94 |
| A | ARG121 |
| A | HOH445 |
| A | HOH700 |
| I | DC8 |
| I | DG9 |
| A | ARG65 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 269 |
| Chain | Residue |
| A | ARG140 |
| A | GLY143 |
| A | ARG144 |
| A | ASN145 |
| A | ASN227 |
| A | GLU229 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 270 |
| Chain | Residue |
| A | LYS20 |
| A | GLY21 |
| A | TRP25 |
| A | MET244 |
| A | HOH348 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 271 |
| Chain | Residue |
| A | ASN10 |
| A | ASN12 |
| A | GLU38 |
| A | ASP247 |
| A | HIS248 |
| A | HOH504 |
| A | HOH714 |
| A | HOH718 |
| I | DG9 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 266 |
| Chain | Residue |
| B | LYS20 |
| B | TRP25 |
| B | ASP242 |
| B | VAL243 |
| B | MET244 |
| B | HOH317 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 267 |
| Chain | Residue |
| B | ARG65 |
| B | TYR68 |
| B | GLU94 |
| B | MET117 |
| B | ARG121 |
| H | DC8 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 268 |
| Chain | Residue |
| B | ASN10 |
| B | ASN12 |
| B | GLU38 |
| B | ASP247 |
| B | HIS248 |
| B | HOH515 |
| B | HOH715 |
| B | HOH716 |
| H | DG9 |
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 |
