Structure of PDB 5h1z Chain A

Receptor sequence
>5h1zA (length=400) Species: 1112214 (Sphingomonas sp. PAMC 26605) [Search protein sequence]
VIDRFDVSRPELYRDDLWQAPFRELRATAPVHRVEHSDFGPYWSVSSYKP
IITVESLPDLYSSAGGITLADFIENNPTDVRMPMFIAMDRPKHTGQRRTV
APAFTPSEMVRMSDNIRMRTAEVLDSLEWNTPFDWVDTVSVELTTQMLAI
LFDFPWEERRKLTFWSDWAGDIELVKNEELRLERLRHMYECGGYFQNLWN
AKIGKPPTPDLISMMIHSDAMAEMDQMEFLGNLILLIVGGNDTTRNTMSA
VAYGLDLFPDQRAKLEADPSMIPNTVQEIIRWQTPLAHMRRTATVDSELE
GQQIKAGDKLALWYISANRDESVFENADRIIVDRPNARRHLAFGHGIHRC
VGARLAELQIAVLLEEMAKRRMRVNVLGEPERVAACFVHGYRKLPVEISR
3D structure
PDB5h1z Crystal Structure of a Putative Cytochrome P450 Alkane Hydroxylase (CYP153D17) from Sphingomonas sp. PAMC 26605 and Its Conformational Substrate Binding
ChainA
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D177 G245 D248 C356 V394
Catalytic site (residue number reindexed from 1) D171 G239 D242 C350 V388
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A E61 F91 I92 H99 R103 F110 L241 G245 G246 T249 A348 F349 G350 H351 H354 R355 C356 V357 G358 A362 E55 F85 I86 H93 R97 F104 L235 G239 G240 T243 A342 F343 G344 H345 H348 R349 C350 V351 G352 A356
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:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:5h1z, PDBe:5h1z, PDBj:5h1z
PDBsum5h1z
PubMed27941697
UniProtA0A1S4NYE0

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