Structure of PDB 1e1k Chain A

Receptor sequence
>1e1kA (length=455) Species: 9913 (Bos taurus) [Search protein sequence]
TPQICVVGSGPAGFYTAQHLLKHHSRAHVDIYEKQLVPFGLVRFGVAPDH
PEVKNVINTFTQTARSDRCAFYGNVEVGRDVTVQELQDAYHAVVLSYGAE
DHQALDIPGEELPGVFSARAFVGWYNGLPENRELAPDLSCDTAVILGQGN
VALDVARILLTPPDHLEKTDITEAALGALRQSRVKTVWIVGRRGPLQVAF
TIKELREMIQLPGTRPMLDPADFLGLQDRIKEAARPRKRLMELLLRTATE
KPGVEEAARRASASRAWGLRFFRSPQQVLPSPDGRRAAGIRLAVTRLEGI
GEATRAVPTGDVEDLPCGLVLSSIGYKSRPIDPSVPFDPKLGVVPNMEGR
VVDVPGLYCSGWVKRGPTGVITTTMTDSFLTGQILLQDLKAGHLPSGPRP
GSAFIKALLDSRGVWPVSFSDWEKLDAEEVSRGQASGKPREKLLDPQEML
RLLGH
3D structure
PDB1e1k Crystal Structures of Adrenodoxin Reductase in Complex with Nadp+ and Nadph Suggesting a Mechanism for the Electron Transfer of an Enzyme Family
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H55 D159 I376 T377
Catalytic site (residue number reindexed from 1) H50 D154 I371 T372
Enzyme Commision number 1.18.1.6: adrenodoxin-NADP(+) reductase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0015039 NADPH-adrenodoxin reductase activity
GO:0016491 oxidoreductase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0050661 NADP binding
Biological Process
GO:0006694 steroid biosynthetic process
GO:0008203 cholesterol metabolic process
GO:0022900 electron transport chain
GO:0070995 NADPH oxidation
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1e1k, PDBe:1e1k, PDBj:1e1k
PDBsum1e1k
PubMed10998235
UniProtP08165|ADRO_BOVIN NADPH:adrenodoxin oxidoreductase, mitochondrial (Gene Name=FDXR)

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