Structure of PDB 1xet Chain D

Receptor sequence
>1xetD (length=384) Species: 3349 (Pinus sylvestris) [Search protein sequence]
FEGFRKLQRADGFASILAIGTANPPNAVDQSTYPDFYFRITGNEHNDKFK
RICERSAIKQRYMYLTEEILKKNPDVCAFVEVPSLDARQAMLAMEVPRLA
KEAAEKAIQEWGQSKSGITHLIFCSTTTPDLPGADFEVAKLLGLHPSVKR
VGVFQHGCFAGGTVLRMAKDLAENNRGARVLVICSETTAVTFRGPSETHL
DSLVGQALFGDGASALIVGADPIPQVEKACFEIVWTAQTVVPNSEGAIGG
KVREVGLTFQLKGAVPDLISANIENCMVEAFSQFKISDWNKLFWVVHPGG
RAILDRVEAKLNLDPTKLIPTRHVMSEYGNMSSACVHFILDQTRKASLQN
GCSTTGEGLEMGVLFGFGPGLTIETVVLKSVPIQ
3D structure
PDB1xet Crystal structure of stilbene synthase from Pinus sylvestris, complexed with methylmalonyl CoA
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C167 F218 H306 N339
Catalytic site (residue number reindexed from 1) C158 F209 H297 N330
Enzyme Commision number 2.3.1.146: pinosylvin synthase.
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 3IO D C167 F218 I257 L266 F268 H306 F376 C158 F209 I248 L257 F259 H297 F367
BS02 MCA D K57 R60 I61 L209 D210 V213 I257 L270 G308 G309 R310 A311 I312 K48 R51 I52 L200 D201 V204 I248 L261 G299 G300 R301 A302 I303
Gene Ontology
Molecular Function
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0050198 pinosylvin synthase activity
Biological Process
GO:0009058 biosynthetic process
GO:0030639 polyketide biosynthetic 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:1xet, PDBe:1xet, PDBj:1xet
PDBsum1xet
PubMed
UniProtQ02323|DPSS_PINSY Pinosylvin synthase

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