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2D07

Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000700molecular_functionmismatch base pair DNA N-glycosylase activity
A0006285biological_processbase-excision repair, AP site formation
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0016605cellular_componentPML body
B0016925biological_processprotein sumoylation
B0019789molecular_functionSUMO transferase activity
B0031386molecular_functionprotein tag activity
B0031625molecular_functionubiquitin protein ligase binding
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0044389molecular_functionubiquitin-like protein ligase binding
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0098686cellular_componenthippocampal mossy fiber to CA3 synapse
B0098793cellular_componentpresynapse
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0098982cellular_componentGABA-ergic synapse
B0099523cellular_componentpresynaptic cytosol
B0099524cellular_componentpostsynaptic cytosol
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1mug
ChainResidueDetails
AASN140

site_idMCSA1
Number of Residues2
DetailsM-CSA 834
ChainResidueDetails
AASN140electrostatic interaction
AHIS151proton acceptor, proton donor

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PDB entries from 2025-11-05

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