Structure of PDB 1ipe Chain B

Receptor sequence
>1ipeB (length=259) Species: 4076 (Datura stramonium) [Search protein sequence]
AGRWNLEGCTALVTGGSRGIGYGIVEELASLGASVYTCSRNQKELNDCLT
QWRSKGFKVEASVCDLSSRSERQELMNTVANHFHGKLNILVNNAGIVIYK
EAKDYTVEDYSLIMSINFEAAYHLSVLAHPFLKASERGNVVFISSVSGAL
AVPYEAVYGATKGAMDQLTRCLAFEWAKDNIRVNGVGPGVIATSLVEMTI
QDPEQKENLNKLIDRCALRRMGEPKELAAMVAFLCFPAASYVTGQIIYVD
GGLMANCGF
3D structure
PDB1ipe Capturing Enzyme Structure Prior to Reaction Initiation: Tropinone Reductase-II-Substrate Complexes
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G20 S146 Y159 K163
Catalytic site (residue number reindexed from 1) G19 S145 Y158 K162
Enzyme Commision number 1.1.1.236: tropinone reductase II.
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 NDP B G16 S18 R19 G20 I21 S40 R41 C65 D66 L67 N94 G96 S146 Y159 K163 P189 I192 T194 S195 L196 G15 S17 R18 G19 I20 S39 R40 C64 D65 L66 N93 G95 S145 Y158 K162 P188 I191 T193 S194 L195
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0050358 tropinone reductase activity
Biological Process
GO:0009710 tropane alkaloid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1ipe, PDBe:1ipe, PDBj:1ipe
PDBsum1ipe
PubMed12741812
UniProtP50163|TRN2_DATST Tropinone reductase 2 (Gene Name=TR2)

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