Structure of PDB 3ihg Chain C Binding Site BS02

Receptor Information
>3ihg Chain C (length=535) Species: 1924 (Streptomyces purpurascens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNDHEVDVLVVGAGLGGLSTAMFLARQGVRVLVVERRPGLSPYPRAAGQN
PRTMELLRIGGVADEVVRADDIRGTQGDFVIRLAESVRGEILRTVSESFD
DMVAATEPCTPAGWAMLSQDKLEPILLAQARKHGGAIRFGTRLLSFRQHD
DDAGAGVTARLAGPDGEYDLRAGYLVGADGNRSLVRESLGIGRYGHGTLT
HMVGVIFDADLSGIMEPGTTGWYYLHHPEFKGTFGPTDRPDRHTLFVEYD
PDEGERPEDFTPQRCVELIGLALDAPEVKPELVDIQGWEMAARIAERWRE
GRVFLAGDAAKVTPPTGGMSGNAAVADGFDLAWKLAAVLQGQAGAGLLDT
YEDERKVAAELVVAEALAIYAQRMAPHMAEVWDKSVGYPETLLGFRYRSS
AVLATDDDPARVENPLTPSGRPGFRGPHVLVSRHGERLSTVDLFGDGWTL
LAGELGADWVAAAEAVSAELGVPVRAYRVGAGLTDPESAVSERYGIGKAG
ASLVRPDGIVAWRTDEAAADAAQTLEGVLRRVLDR
Ligand information
Ligand IDVAK
InChIInChI=1S/C22H20O8/c1-3-22(29)8-13(24)15-10(17(22)21(28)30-2)7-11-16(20(15)27)19(26)14-9(18(11)25)5-4-6-12(14)23/h4-7,13,17,23-24,27,29H,3,8H2,1-2H3/t13-,17-,22+/m0/s1
InChIKeyRACGRCLGVYXIAO-YOKWENHESA-N
SMILES
SoftwareSMILES
CACTVS 3.352CC[C]1(O)C[CH](O)c2c(O)c3C(=O)c4c(O)cccc4C(=O)c3cc2[CH]1C(=O)OC
ACDLabs 11.02O=C(OC)C4c2c(c(O)c1C(=O)c3c(C(=O)c1c2)cccc3O)C(O)CC4(O)CC
OpenEye OEToolkits 1.7.0CCC1(CC(c2c(cc3c(c2O)C(=O)c4c(cccc4O)C3=O)C1C(=O)OC)O)O
CACTVS 3.352CC[C@@]1(O)C[C@H](O)c2c(O)c3C(=O)c4c(O)cccc4C(=O)c3cc2[C@H]1C(=O)OC
OpenEye OEToolkits 1.7.0CC[C@]1(C[C@@H](c2c(cc3c(c2O)C(=O)c4c(cccc4O)C3=O)[C@H]1C(=O)OC)O)O
FormulaC22 H20 O8
Namemethyl (1R,2R,4S)-2-ethyl-2,4,5,7-tetrahydroxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate;
Aklavinone
ChEMBL
DrugBank
ZINCZINC000004654750
PDB chain3ihg Chain C Residue 537 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3ihg Structural basis for substrate recognition and specificity in aklavinone-11-hydroxylase from rhodomycin biosynthesis.
Resolution2.49 Å
Binding residue
(original residue number in PDB)
A47 F79 M202 W222 Y224 P315 T316 G317 G318
Binding residue
(residue number reindexed from 1)
A47 F79 M202 W222 Y224 P315 T316 G317 G318
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) A47 F234 F246 P315
Catalytic site (residue number reindexed from 1) A47 F234 F246 P315
Enzyme Commision number 1.14.13.180: aklavinone 12-hydroxylase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
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:0071949 FAD binding
Biological Process
GO:0006744 ubiquinone biosynthetic process
GO:0017000 antibiotic biosynthetic process
GO:1901771 daunorubicin biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3ihg, PDBe:3ihg, PDBj:3ihg
PDBsum3ihg
PubMed19744497
UniProtQ54530|DNRF_STREF Aklavinone 12-hydroxylase RdmE (Gene Name=rdmE)

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