Structure of PDB 8cvg Chain A

Receptor sequence
>8cvgA (length=327) Species: 33113 (Atropa belladonna) [Search protein sequence]
VSESFVAPLEKRAENDVPLGNDVPIIDLQQDHLVVVQQITKACQDFGLFQ
VINHGLPEKLMAETMDVCKEFFALPAEEKEKLQPKGEPAKFELPLEQKAK
LYVEGEQLEAFLYWKDTLAHGCHPLDEELVNSWPEKPATYREVVAKYSVE
VRKLTMRILDYICEGLGLKLGYFDNELSQIQMMLTNYYPPCPDPSSTLGS
GGHYDGNLITLLQQNLPGLQQLIDAKWIAVEPIPTAFVVNLGLTLKVITN
EKFEGSIHRVVTNPTRDRVSIATFIGPDYSCTIEPAKELLSQDNPPLYKP
YSYAEFGEIYLSDKSDYDAGVKPYKIN
3D structure
PDB8cvg Structure of the L289F H6H cyclization reactant complex
ChainA
Resolution1.56 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.11: hyoscyamine (6S)-dioxygenase.
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 FE2 A H217 D219 H273 H203 D205 H258
BS02 AKG A N200 Y202 H217 H273 V275 R283 S285 F289 N186 Y188 H203 H258 V260 R268 S270 F274
BS03 OVR A F103 E116 L198 H217 G220 F289 Y318 Y325 L326 F91 E104 L184 H203 G206 F274 Y303 Y310 L311
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016706 2-oxoglutarate-dependent dioxygenase activity
GO:0031418 L-ascorbic acid binding
GO:0046872 metal ion binding
GO:0047998 hyoscyamine (6S)-dioxygenase activity
Biological Process
GO:0002238 response to molecule of fungal origin
GO:0009805 coumarin biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:8cvg, PDBe:8cvg, PDBj:8cvg
PDBsum8cvg
PubMed
UniProtQ9XJ43

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