Structure of PDB 1xes Chain B

Receptor sequence
>1xesB (length=387) Species: 3349 (Pinus sylvestris) [Search protein sequence]
FEGFRKLQRADGFASILAIGTANPPNAVDQSTYPDFYFRITGNEHNTELK
DKFKRICERSAIKQRYMYLTEEILKKNPDVCAFVEVPSLDARQAMLAMEV
PRLAKEAAEKAIQEWGQSKSGITHLIFCSTTTPDLPGADFEVAKLLGLHP
SVKRVGVFQHGCFAGGTVLRMAKDLAENNRGARVLVICSETTAVTFRGPS
ETHLDSLVGQALFGDGASALIVGADPIPQVEKACFEIVWTAQTVVPNSEG
AIGGKVREVGLTFQLKGAVPDLISANIENCMVEAFSQFKISDWNKLFWVV
HPGGRAILDRVEAKLNLDPTKLIPTRHVMSEYGNMSSACVHFILDQTRKA
SLQNGCSTTGEGLEMGVLFGFGPGLTIETVVLKSVPI
3D structure
PDB1xes Crystal structure of stilbene synthase from Pinus sylvestris
ChainB
Resolution1.7 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) C162 F213 H301 N334
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 B C167 F218 I257 F268 C162 F213 I252 F263
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:1xes, PDBe:1xes, PDBj:1xes
PDBsum1xes
PubMed
UniProtQ02323|DPSS_PINSY Pinosylvin synthase

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