Structure of PDB 1xes Chain D

Receptor sequence
>1xesD (length=382) Species: 3349 (Pinus sylvestris) [Search protein sequence]
FEGFRKLQRADGFASILAIGTANPPNAVDQSTYPDFYFRITGNELKDKFK
RICSAIKQRYMYLTEEILKKNPDVCAFVEVPSLDARQAMLAMEVPRLAKE
AAEKAIQEWGQSKSGITHLIFCSTTTPDLPGADFEVAKLLGLHPSVKRVG
VFQHGCFAGGTVLRMAKDLAENNRGARVLVICSETTAVTFRGPSETHLDS
LVGQALFGDGASALIVGADPIPQVEKACFEIVWTAQTVVPNSEGAIGGKV
REVGLTFQLKGAVPDLISANIENCMVEAFSQFKISDWNKLFWVVHPGGRA
ILDRVEAKLNLDPTKLIPTRHVMSEYGNMSSACVHFILDQTRKASLQNGC
STTGEGLEMGVLFGFGPGLTIETVVLKSVPIQ
3D structure
PDB1xes Crystal structure of stilbene synthase from Pinus sylvestris
ChainD
Resolution1.7 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) C167 F218 H306 N339
Catalytic site (residue number reindexed from 1) C156 F207 H295 N328
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 G258 F268 H306 C156 F207 I246 G247 F257 H295
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1xes, PDBe:1xes, PDBj:1xes
PDBsum1xes
PubMed
UniProtQ02323|DPSS_PINSY Pinosylvin synthase

[Back to BioLiP]