Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8DW7

DNA glycosylase MutY variant N146S in complex with DNA containing the transition state analog 1N paired with d(8-oxo-G)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000701molecular_functionpurine-specific mismatch base pair DNA N-glycosylase activity
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006298biological_processmismatch repair
A0006950biological_processresponse to stress
A0006974biological_processDNA damage response
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019104molecular_functionDNA N-glycosylase activity
A0032357molecular_functionoxidized purine DNA binding
A0034039molecular_function8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
A0035485molecular_functionadenine/guanine mispair binding
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
D0000701molecular_functionpurine-specific mismatch base pair DNA N-glycosylase activity
D0003677molecular_functionDNA binding
D0003824molecular_functioncatalytic activity
D0006281biological_processDNA repair
D0006284biological_processbase-excision repair
D0006298biological_processmismatch repair
D0006950biological_processresponse to stress
D0006974biological_processDNA damage response
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0019104molecular_functionDNA N-glycosylase activity
D0032357molecular_functionoxidized purine DNA binding
D0034039molecular_function8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
D0035485molecular_functionadenine/guanine mispair binding
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsDomain: {"description":"HhH","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14961129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"14961129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25995449","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2009","submissionDatabase":"PDB data bank","title":"Structural illumination of a mutY glycosylase reaction coordinate intermediate.","authors":["O'Shea V.L.","Cao S.","Richards J.L.","Horvath M.P.","David S.S."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2015","submissionDatabase":"PDB data bank","title":"Structure and stereochemistry of the base excision repair glycosylase MutY reveal a mechanism similar to retaining glycosidases.","authors":["Woods R.D.","O'Shea V.L.","Chu A.","Cao S.","Richards J.L.","Horvath M.P.","David S.S."]}},{"source":"PDB","id":"1RRQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1RRS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1VRL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"19841264","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25995449","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 807
ChainResidueDetails
AGLU43activator, proton acceptor, proton donor
ATYR126electrostatic stabiliser
AASP144covalently attached, nucleofuge, nucleophile

site_idMCSA2
Number of Residues3
DetailsM-CSA 807
ChainResidueDetails
DGLU43activator, proton acceptor, proton donor
DTYR126electrostatic stabiliser
DASP144covalently attached, nucleofuge, nucleophile

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon