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1OWL

Structure of apophotolyase from Anacystis nidulans

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
A0009416biological_processresponse to light stimulus
A0016829molecular_functionlyase activity
A0071949molecular_functionFAD binding
A0097159molecular_functionorganic cyclic compound binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 486
ChainResidue
AARG11
AHOH825
AILE41
AMET47
AARG51
ALYS248
APHE249
AHOH772
AHOH776
AHOH803

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 487
ChainResidue
ASER16
AARG65
ATHR167
AHOH806

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE FAD A 485
ChainResidue
ATYR228
ATHR240
ASER241
AGLY242
ALEU243
ASER244
ALEU247
ATRP280
AGLU283
AARG287
ATYR290
ATRP346
AMET347
AASN349
AARG352
ALEU378
AASP380
AGLY381
AASP382
AALA385
AASN386
AGLY389
AHOH498
AHOH520
AHOH529
AHOH546
AHOH644
AHOH730

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dnp
ChainResidueDetails
ATRP314
ATRP390
ATRP367

227344

PDB entries from 2024-11-13

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