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2END

CRYSTAL STRUCTURE OF A PYRIMIDINE DIMER SPECIFIC EXCISION REPAIR ENZYME FROM BACTERIOPHAGE T4: REFINEMENT AT 1.45 ANGSTROMS AND X-RAY ANALYSIS OF THE THREE ACTIVE SITE MUTANTS

Replaces:  1END
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
A0008152biological_processmetabolic process
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
DetailsACT_SITE: Nucleophile; via amide nitrogen => ECO:0000269|PubMed:8347626, ECO:0007744|PDB:1VAS
ChainResidueDetails
ATHR2

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:8347626, ECO:0007744|PDB:1VAS
ChainResidueDetails
AGLU23

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Substrate binding => ECO:0000269|PubMed:1409651, ECO:0000269|PubMed:7783199
ChainResidueDetails
AARG3

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Substrate binding => ECO:0000269|PubMed:1409651
ChainResidueDetails
AARG22
AARG117
ALYS121

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0007744|PDB:1VAS
ChainResidueDetails
AARG26

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 162
ChainResidueDetails
ATHR2covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AARG22electrostatic stabiliser, hydrogen bond donor
AGLU23hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG26electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-04-24

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