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1IB0

CRYSTAL STRUCTURE OF RAT B5R IN COMPLEX WITH FAD AND NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD A 301
ChainResidue
AHIS77
APHE113
APHE120
AGLY123
AGLY124
ALYS125
AMET126
ASER127
ATHR181
ATHR184
APRO185
AARG91
AHOH337
AHOH338
AHOH418
ANAD1994
APRO92
ATYR93
ATHR94
AVAL108
AVAL109
ALYS110
ATYR112

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD A 1994
ChainResidue
ALYS110
ATYR112
ATHR181
AGLY182
AALA208
AASN209
AGLN210
AASP239
APHE251
AGLY274
APRO275
APRO276
APRO277
AMET278
AFAD301
AHOH356
AHOH397
AHOH419

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues112
DetailsDomain: {"description":"FAD-binding FR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00716","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11695905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IB0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00387","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00387","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCN2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
ATYR93

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PDB entries from 2025-07-23

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