Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8DWF

Glycosylase MutY variant E43S in complex with DNA containing d(8-oxo-G) paired with substrate adenine

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
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
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
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
D0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:19841264
ChainResidueDetails
ASER43
DSER43

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19841264
ChainResidueDetails
ATRP30
ATYR126
AGLU188
DTRP30
DTYR126
DGLU188

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:14961129, ECO:0000269|PubMed:19841264
ChainResidueDetails
AGLN48
ALEU86
ASER308
DGLN48
DLEU86
DSER308

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:14961129, ECO:0000269|PubMed:19841264, ECO:0000269|PubMed:25995449, ECO:0000269|Ref.3, ECO:0000269|Ref.5, ECO:0007744|PDB:1RRQ, ECO:0007744|PDB:1RRS, ECO:0007744|PDB:1VRL
ChainResidueDetails
ACYS198
ACYS205
ACYS208
ACYS214
DCYS198
DCYS205
DCYS208
DCYS214

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:19841264, ECO:0000305|PubMed:25995449
ChainResidueDetails
AASP144
DASP144

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 807
ChainResidueDetails
ASER43activator, proton acceptor, proton donor
ATYR126electrostatic stabiliser
AASP144covalently attached, nucleofuge, nucleophile

site_idMCSA2
Number of Residues3
DetailsM-CSA 807
ChainResidueDetails
DSER43activator, proton acceptor, proton donor
DTYR126electrostatic stabiliser
DASP144covalently attached, nucleofuge, nucleophile

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon