Structure of PDB 3ihg Chain A

Receptor sequence
>3ihgA (length=535) Species: 1924 (Streptomyces purpurascens) [Search protein sequence]
MNDHEVDVLVVGAGLGGLSTAMFLARQGVRVLVVERRPGLSPYPRAAGQN
PRTMELLRIGGVADEVVRADDIRGTQGDFVIRLAESVRGEILRTVSESFD
DMVAATEPCTPAGWAMLSQDKLEPILLAQARKHGGAIRFGTRLLSFRQHD
DDAGAGVTARLAGPDGEYDLRAGYLVGADGNRSLVRESLGIGRYGHGTLT
HMVGVIFDADLSGIMEPGTTGWYYLHHPEFKGTFGPTDRPDRHTLFVEYD
PDEGERPEDFTPQRCVELIGLALDAPEVKPELVDIQGWEMAARIAERWRE
GRVFLAGDAAKVTPPTGGMSGNAAVADGFDLAWKLAAVLQGQAGAGLLDT
YEDERKVAAELVVAEALAIYAQRMAPHMAEVWDKSVGYPETLLGFRYRSS
AVLATDDDPARVENPLTPSGRPGFRGPHVLVSRHGERLSTVDLFGDGWTL
LAGELGADWVAAAEAVSAELGVPVRAYRVGAGLTDPESAVSERYGIGKAG
ASLVRPDGIVAWRTDEAAADAAQTLEGVLRRVLDR
3D structure
PDB3ihg Structural basis for substrate recognition and specificity in aklavinone-11-hydroxylase from rhodomycin biosynthesis.
ChainA
Resolution2.49 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) 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.
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 FAD A G12 G14 E35 R36 R45 A46 Q119 R142 L143 D179 G180 W288 G307 D308 G12 G14 E35 R36 R45 A46 Q119 R142 L143 D179 G180 W288 G307 D308
BS02 VAK A A47 F79 M202 W222 Y224 P315 T316 G317 G318 A47 F79 M202 W222 Y224 P315 T316 G317 G318
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)

[Back to BioLiP]