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1QNF

STRUCTURE OF PHOTOLYASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003677molecular_functionDNA binding
A0003904molecular_functiondeoxyribodipyrimidine photo-lyase activity
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0006281biological_processDNA repair
A0006950biological_processresponse to stress
A0006974biological_processDNA damage response
A0016829molecular_functionlyase activity
A0032922biological_processcircadian regulation of gene expression
A0043153biological_processentrainment of circadian clock by photoperiod
A0051716biological_processcellular response to stimulus
A0071949molecular_functionFAD binding
A0097159molecular_functionorganic cyclic compound binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD A 485
ChainResidue
ATYR228
AARG287
ATRP346
AASN349
AARG352
AASP380
AGLY381
AASP382
AALA385
AASN386
AHOH578
ATHR240
AHOH601
AHOH616
AHOH631
AHOH632
AHOH634
ASER241
AGLY242
ALEU243
ASER244
ALEU247
ATRP280
AGLU283

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HDF A 486
ChainResidue
AARG10
APHE35
ACYS36
ALEU37
AASP38
AILE41
AMET47
AARG51
ALEU55
AASP101
AGLU103
AGLY106
AARG109
ALYS248
APHE249
AHOH635
AHOH636
AHOH637
AHOH647

Functional Information from PROSITE/UniProt
site_idPS00394
Number of Residues13
DetailsDNA_PHOTOLYASES_1_1 DNA photolyases class 1 signature 1. TGyPIVDAaMRqL
ChainResidueDetails
ATHR329-LEU341

site_idPS00691
Number of Residues20
DetailsDNA_PHOTOLYASES_1_2 DNA photolyases class 1 signature 2. NRcRMIvASFLtKdLiidWR
ChainResidueDetails
AASN349-ARG368

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING:
ChainResidueDetails
ALEU37
AVAL52
AILE102
AASN233
APHE249
AALA412
AALA473

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15213381, ECO:0000269|PubMed:15576622, ECO:0000269|PubMed:9360600
ChainResidueDetails
AASP229
ASER241
AMET347
AGLY381
AASN387

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Electron transfer via tryptophanyl radical => ECO:0000250
ChainResidueDetails
AGLU315
AARG368
AGLN391

218853

PDB entries from 2024-04-24

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