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1IQR

Crystal structure of DNA photolyase from Thermus thermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003677molecular_functionDNA binding
A0003904molecular_functiondeoxyribodipyrimidine photo-lyase activity
A0006139biological_processnucleobase-containing compound metabolic process
A0006281biological_processDNA repair
A0006950biological_processresponse to stress
A0006974biological_processDNA damage response
A0009416biological_processresponse to light stimulus
A0016829molecular_functionlyase activity
A0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 422
ChainResidue
AARG9
AGLY10
ASER96
AARG104
AHOH424

site_idAC2
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD A 421
ChainResidue
ALEU212
ASER213
APHE216
ATRP241
AGLU244
ATRP247
AARG248
APHE307
ALEU308
AASN310
AARG313
AALA317
ALEU339
AASP341
AGLY342
AASP343
AVAL346
AASN347
AGLN349
AGLY350
AHOH440
AHOH457
AHOH475
AHOH494
ATYR197
AGLY209
ASER210
AARG211

Functional Information from PROSITE/UniProt
site_idPS00394
Number of Residues13
DetailsDNA_PHOTOLYASES_1_1 DNA photolyases class 1 signature 1. TGvPLVDAaMReL
ChainResidueDetails
ATHR290-LEU302

site_idPS00691
Number of Residues20
DetailsDNA_PHOTOLYASES_1_2 DNA photolyases class 1 signature 2. NRaRMNaAQFAvKhLllpWK
ChainResidueDetails
AASN310-LYS329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues122
DetailsDomain: {"description":"Photolyase/cryptochrome alpha/beta"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues29
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsRegion: {"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues11
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11707580","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsSite: {"description":"Electron transfer via tryptophanyl radical","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dnp
ChainResidueDetails
ATRP328
ATRP275
ATRP351

249697

PDB entries from 2026-02-25

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