Structure of PDB 5e58 Chain D

Receptor sequence
>5e58D (length=463) Species: 56216 (Neotoma lepida) [Search protein sequence]
LPPGPRPLPLLGNLLQMDRGGFLNSFMRIREKYGDVFTVHLGPRPVVMLY
GTEAIREALVDQAEAFSGRGTIAVIKPVIGDYGMIFSNGERWKVLRRFSL
ATMRDFGMGKSVEDRIQEEAQCLVEELQKSQGAPLDPTFLFQCITANIIC
SIVFGERYDYKDRQFLRLLDLFYRTFSLMSSFSSQVFELFSGFMKYFPGA
HRQITRNLQEILDYVGQSVEKHRATLDPSNPRDFIDTYLLRMEKEKSNQH
TEFHHQNLLISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQ
VIGSHRLPTLEDRTKMPYTDAVIHEIQRFSDLAPIGAPHKVTKDTLFRGY
LLPKNTEVYPILSSALHDPQYFEQPGTFNPDHFLDANGALKKSEAFMPFS
IGKRICLGEGIARNELFLFFTTILQNFSVSSSVAPKDIDLSPKESGIGKV
PQTYQISFLARHH
3D structure
PDB5e58 Structure-Function Analysis of Mammalian CYP2B Enzymes Using 7-Substituted Coumarin Derivatives as Probes: Utility of Crystal Structures and Molecular Modeling in Understanding Xenobiotic Metabolism.
ChainD
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T302 F429 C436
Catalytic site (residue number reindexed from 1) T272 F399 C406
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
GO:0020037 heme binding

View graph for
Molecular Function
External links
PDB RCSB:5e58, PDBe:5e58, PDBj:5e58
PDBsum5e58
PubMed26826176
UniProtJ9JD66

[Back to BioLiP]