3W2Y
Crystal structure of DNA uridine endonuclease Mth212 mutant W205S
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 |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003906 | molecular_function | DNA-(apurinic or apyrimidinic site) endonuclease activity |
| D | 0004518 | molecular_function | nuclease activity |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0006281 | biological_process | DNA repair |
| D | 0006284 | biological_process | base-excision repair |
| D | 0006974 | biological_process | DNA damage response |
| D | 0008081 | molecular_function | phosphoric diester hydrolase activity |
| D | 0008311 | molecular_function | double-stranded DNA 3'-5' DNA exonuclease activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | ASN12 |
| A | GLU38 |
| A | HOH411 |
| A | HOH468 |
| A | HOH509 |
| A | HOH590 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 302 |
| Chain | Residue |
| A | PHE86 |
| A | HOH594 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 303 |
| Chain | Residue |
| A | ASN187 |
| A | HOH495 |
| D | GLN45 |
| A | LYS183 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 304 |
| Chain | Residue |
| A | PRO43 |
| A | PHE59 |
| A | PHE60 |
| A | GLU214 |
| A | HOH431 |
| A | HOH558 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 305 |
| Chain | Residue |
| A | GLU158 |
| A | ARG178 |
| A | HOH613 |
| D | ASN114 |
| D | LYS116 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 306 |
| Chain | Residue |
| A | ARG236 |
| A | HOH447 |
| A | HOH614 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 308 |
| Chain | Residue |
| A | LYS116 |
| A | ASN153 |
| A | SER171 |
| A | TRP219 |
| A | HOH413 |
| A | HOH579 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 309 |
| Chain | Residue |
| A | TYR208 |
| A | MET244 |
| A | GLY245 |
| A | SER246 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 310 |
| Chain | Residue |
| A | ARG194 |
| A | MET195 |
| A | PHE196 |
| A | SER198 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 311 |
| Chain | Residue |
| A | LYS40 |
| A | TYR68 |
| A | SER69 |
| A | TYR111 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 312 |
| Chain | Residue |
| A | ARG163 |
| A | ASN167 |
| A | TRP219 |
| A | HOH435 |
| A | HOH479 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 313 |
| Chain | Residue |
| A | HIS156 |
| A | ARG157 |
| A | ILE185 |
| A | HOH430 |
| A | HOH456 |
| A | HOH581 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 301 |
| Chain | Residue |
| D | ASN12 |
| D | GLU38 |
| D | HOH407 |
| D | HOH425 |
| D | HOH430 |
| D | HOH449 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT D 302 |
| Chain | Residue |
| D | ARG157 |
| D | GLU158 |
| D | ILE159 |
| D | ARG178 |
| D | HOH525 |
| D | HOH535 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT D 303 |
| Chain | Residue |
| D | MET195 |
| D | SER198 |
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 |
