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3UMV

Eukaryotic Class II CPD photolyase structure reveals a basis for improved UV-tolerance in plants

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000719biological_processphotoreactive repair
A0003677molecular_functionDNA binding
A0003904molecular_functiondeoxyribodipyrimidine photo-lyase activity
A0003913molecular_functionDNA photolyase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0006139biological_processnucleobase-containing compound metabolic process
A0006281biological_processDNA repair
A0006950biological_processresponse to stress
A0006974biological_processDNA damage response
A0009650biological_processUV protection
A0016829molecular_functionlyase activity
A0071949molecular_functionFAD binding
B0000166molecular_functionnucleotide binding
B0000719biological_processphotoreactive repair
B0003677molecular_functionDNA binding
B0003904molecular_functiondeoxyribodipyrimidine photo-lyase activity
B0003913molecular_functionDNA photolyase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0006139biological_processnucleobase-containing compound metabolic process
B0006281biological_processDNA repair
B0006950biological_processresponse to stress
B0006974biological_processDNA damage response
B0009650biological_processUV protection
B0016829molecular_functionlyase activity
B0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 701
ChainResidue
ATRP241
AGLY283
AHIS388
ALYS390
AHOH691
AURE901

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 703
ChainResidue
AGLN447
AHOH871
AHOH918
AHOH952
ASER184
AASP221
AHIS445

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 705
ChainResidue
AARG46
ASER138
ALEU140
APRO431
AHOH702
AHOH779
AHOH935

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 706
ChainResidue
AGLU405
AARG452
APRO453
AHOH1293

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 707
ChainResidue
AASP148
AHOH655

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 708
ChainResidue
APRO78
AARG79
AHOH802

site_idAC7
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD A 801
ChainResidue
ATYR268
ALEU281
ASER282
AGLY283
ALEU284
ASER285
ALEU288
AGLU319
ALEU320
AARG323
AARG324
ALYS390
AGLY393
AARG396
AASN421
AASP427
AGLY428
ASER432
AGLY433
AGLY436
AHOH633
AHOH696
AHOH697
AHOH698
AHOH704
AHOH710
AHOH720
AHOH817
AHOH822
AHOH1047

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE URE A 901
ChainResidue
APRO278
AGLU384
ALYS390
AHIS392
AEDO701
AHOH760
AHOH1103

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE URE A 902
ChainResidue
ATRP449
ALYS450
AARG452
AGLY456
AILE458
AARG459
ATYR460
AHOH626

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE URE A 903
ChainResidue
AASP221
ALEU225
AHOH920

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE URE A 904
ChainResidue
APHE74
AALA75
ALEU76
APHE77
ALEU82
ALEU93
AHOH769
AHOH894

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE URE A 905
ChainResidue
APHE112
ALEU113
APHE114
APRO217
AGLU218
AHOH578
AHOH825
AHOH1027

site_idBC4
Number of Residues31
DetailsBINDING SITE FOR RESIDUE FAD B 801
ChainResidue
BLEU288
BGLU319
BLEU320
BARG323
BARG324
BLYS390
BGLY393
BARG396
BMET397
BASN421
BASP427
BGLY428
BSER432
BGLY433
BGLY436
BSER440
BHOH707
BHOH720
BHOH722
BHOH726
BHOH728
BHOH736
BHOH813
BHOH822
BHOH828
BTYR268
BLEU281
BSER282
BGLY283
BLEU284
BSER285

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE URE B 901
ChainResidue
BPRO278
BGLU384
BLYS390
BHIS392
BHOH737

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE URE B 902
ChainResidue
BTRP449
BLYS450
BARG452
BILE458
BARG459
BTYR460

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE URE B 904
ChainResidue
BPHE74
BALA75
BLEU76
BPHE77
BLEU82
BLEU93
BHOH785
BHOH875

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE URE B 905
ChainResidue
BPHE112
BLEU113
BPHE114
BGLU218
BHOH830

Functional Information from PROSITE/UniProt
site_idPS01083
Number of Residues15
DetailsDNA_PHOTOLYASES_2_1 DNA photolyases class 2 signature 1. FlEElVVRRELadNF
ChainResidueDetails
APHE316-PHE330

site_idPS01084
Number of Residues20
DetailsDNA_PHOTOLYASES_2_2 DNA photolyases class 2 signature 2. GlHDqgWkERpVFGKIRYMN
ChainResidueDetails
AGLY443-ASN462

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:22170053, ECO:0007744|PDB:3UMV
ChainResidueDetails
ATYR268
BASP427
ASER282
ALYS390
AASN421
AASP427
BTYR268
BSER282
BLYS390
BASN421

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00914
ChainResidueDetails
AGLU319
BGLU319

site_idSWS_FT_FI3
Number of Residues6
DetailsSITE: Electron transfer via tryptophanyl radical => ECO:0000255
ChainResidueDetails
ATRP378
ATRP399
ATRP406
BTRP378
BTRP399
BTRP406

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18235036
ChainResidueDetails
ASER312
BSER312

218853

PDB entries from 2024-04-24

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