Structure of PDB 2zbz Chain A Binding Site BS01

Receptor Information
>2zbz Chain A (length=404) Species: 1909 (Streptomyces griseolus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWV
VTKHEAARKLLGDPRLSSNRTDDNFPATSPAFEAVRESPQAFIGLDPPEH
GTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALP
VPSMVICRLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGL
ITQFQTEPGAGLVGALVADQLANGEIDREELISTAMLLLIAGHETTASMT
SLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADI
EVEGQLIRAGEGVIVVNSIANRDGTVYEDPDALDIHRSARHHLAFGFGVH
QCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVNELP
VTWH
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain2zbz Chain A Residue 413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2zbz Crystal Structure of CYP105A1 (P450SU-1) in Complex with 1alpha,25-Dihydroxyvitamin D3
Resolution1.9 Å
Binding residue
(original residue number in PDB)		F95 I96 H103 R107 L241 A244 T248 T249 I290 A294 R297 A347 F348 H353 C355 L356 G357
Binding residue
(residue number reindexed from 1)		F92 I93 H100 R104 L238 A241 T245 T246 I287 A291 R294 A344 F345 H350 C352 L353 G354
Annotation score1
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.
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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