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1U3D

Crystal Structure of the PHR domain of Cryptochrome 1 from Arabidopsis thaliana with AMPPNP bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0009785biological_processblue light signaling pathway
A0009882molecular_functionblue light photoreceptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 514
ChainResidue
AANP511

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 515
ChainResidue
AASN238
AARG239
ATHR246
AHIS358

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 516
ChainResidue
ALYS241
ASER244
ATHR246

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 517
ChainResidue
ALYS222
ANDS512
AASN219

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 518
ChainResidue
AHIS318

site_idAC6
Number of Residues27
DetailsBINDING SITE FOR RESIDUE FAD A 510
ChainResidue
ATYR235
ATHR247
ASER248
APHE249
ALEU250
ASER251
ALEU254
APHE290
ASER293
AARG297
ATRP356
AASP359
AARG362
AVAL363
ASER366
ALEU388
AASP390
AALA391
AASP392
ASER395
AASP396
AGLY399
AANP511
AHOH520
AHOH522
AHOH542
AHOH594

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ANP A 511
ChainResidue
AARG239
ALEU296
AASP359
AARG360
AVAL363
ATYR402
AASP409
AFAD510
AMG514
AHOH521

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NDS A 512
ChainResidue
AALA212
ATRP213
ASER214
AALA223
APHE249
AHIS253
AMG517

Functional Information from PROSITE/UniProt
site_idPS00394
Number of Residues13
DetailsDNA_PHOTOLYASES_1_1 DNA photolyases class 1 signature 1. TGyPLVDAgMReL
ChainResidueDetails
ATHR339-LEU351

site_idPS00691
Number of Residues20
DetailsDNA_PHOTOLYASES_1_2 DNA photolyases class 1 signature 2. DRiRVVvSSFFvKvLqlpWR
ChainResidueDetails
AASP359-ARG378

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15299148, ECO:0007744|PDB:1U3C, ECO:0007744|PDB:1U3D
ChainResidueDetails
ATYR235
ASER244
ATHR246
ATHR247
AASP359
AASP390

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15299148, ECO:0007744|PDB:1U3C
ChainResidueDetails
AASN238
ALYS241
AHIS358

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15299148, ECO:0007744|PDB:1U3D
ChainResidueDetails
AARG239
ASER293
AASP409

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Involved in electron transfer from the protein surface to the FAD cofactor => ECO:0000269|PubMed:26313597, ECO:0000303|PubMed:22421133
ChainResidueDetails
ATRP324
ATRP400

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Involved in electron transfer from the protein surface to the FAD cofactor => ECO:0000303|PubMed:22421133
ChainResidueDetails
ATRP377

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1dnp
ChainResidueDetails
ATRP400
ATRP377
ATRP324

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PDB entries from 2024-07-24

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