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1VAS

ATOMIC MODEL OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME COMPLEXED WITH A DNA SUBSTRATE: STRUCTURAL BASIS FOR DAMAGED DNA RECOGNITION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000704molecular_functionpyrimidine dimer DNA N-glycosylase activity
A0003824molecular_functioncatalytic activity
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016829molecular_functionlyase activity
A0033959molecular_functiondeoxyribodipyrimidine endonucleosidase activity
A0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile; via amide nitrogen","evidences":[{"source":"PubMed","id":"8347626","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VAS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"8347626","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1VAS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Substrate binding","evidences":[{"source":"PubMed","id":"1409651","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7783199","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Substrate binding","evidences":[{"source":"PubMed","id":"1409651","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PDB","id":"1VAS","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 8419366, 1409651, 1575827, 10423235
ChainResidueDetails
AARG22
ATHR2
AGLN23

site_idMCSA1
Number of Residues4
DetailsM-CSA 162
ChainResidueDetails
CDT214covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

246031

PDB entries from 2025-12-10

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