Structure of PDB 2zbz Chain A

Receptor sequence
>2zbzA (length=404) Species: 1909 (Streptomyces griseolus) [Search protein sequence]
TATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWV
VTKHEAARKLLGDPRLSSNRTDDNFPATSPAFEAVRESPQAFIGLDPPEH
GTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALP
VPSMVICRLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGL
ITQFQTEPGAGLVGALVADQLANGEIDREELISTAMLLLIAGHETTASMT
SLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADI
EVEGQLIRAGEGVIVVNSIANRDGTVYEDPDALDIHRSARHHLAFGFGVH
QCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVNELP
VTWH
3D structure
PDB2zbz Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1alpha,25-Dihydroxyvitamin D3
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q182 A244 E247 T248 T249 A291 C355 L356 G357 E364 I396
Catalytic site (residue number reindexed from 1) Q179 A241 E244 T245 T246 A288 C352 L353 G354 E361 I393
Enzyme Commision number 1.14.15.22: vitamin D 1,25-hydroxylase.
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:0016709 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0070640 vitamin D3 metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2zbz, PDBe:2zbz, PDBj:2zbz
PDBsum2zbz
PubMed18314962
UniProtP18326|CPXE_STRGO Vitamin D3 dihydroxylase (Gene Name=cyp105A1)

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