Structure of PDB 3sdu Chain A

Receptor sequence
>3sduA (length=780) Species: 46611 (Abies grandis) [Search protein sequence]
WGYDLVHSLKSPYIDSSYRERAEVLVSEIKAMLNPAITGDGESMITPSAY
DTAWVARVPAIDGSARPQFPQTVDWILKNQLKDGSWGIQSHFLLSDRLLA
TLSCVLVLLKWNVGDLQVEQGIEFIKSNLELVKDETDQDSLVTDFEIIFP
SLLREAQSLRLGLPYDLPYIHLLQTKRQERLAKLSREEIYAVPSPLLYSL
EGIQDIVEWERIMEVQSQDGSFLSSPASTACVFMHTGDAKCLEFLNSVMI
KFGNFVPCLYPVDLLERLLIVDNIVRLGIYRHFEKEIKEALDYVYRHWNE
RGIGWGRLNPIADLETTALGFRLLRLHRYNVSPAIFDNFKDAFICSTGQF
NKDVASMLNLYRASQLAFPGENILDEAKSFATKYLREALEKSETSSAWNN
KQNLSQEIKYALKTSWHASVPRVEAKRYCQVYRPDYARIAKCVYKLPYVN
NEKFLELGKLDFNIIQSIHQEEMKNVTSWFRDSGLPLFTFARERPLEFYF
LVAAGTYEPQYAKCRFLFTKVACLQTVLDDMYDTYGTLDELKLFTEAVRR
WDLSFTENLPDYMKLCYQIYYDIVHEVAWEAEKEQGRELVSFFRKGWEDY
LLGYYEEAEWLAAEYVPTLDEYIKNGITSIGQRILLLSGVLIMDGQLLSQ
EALEKVDYPGRRVLTELNSLISRLADDTKTYKAEKARGELASSIECYMKD
HPECTEEEALDHIYSILEPAVKELTREFLKPDDVPFACKKMLFEETRVTM
VIFKDGDGFGVSKLEVKDHIKECLIEPLPL
3D structure
PDB3sdu Structure of a three-domain sesquiterpene synthase: a prospective target for advanced biofuels production.
ChainA
Resolution1.89 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R529 L538 A559 D566 D570 S666 I667 G668 R710 D713 T717 E721 F790 D794 F796
Catalytic site (residue number reindexed from 1) R492 L501 A522 D529 D533 S629 I630 G631 R673 D676 T680 E684 F753 D757 F759
Enzyme Commision number 4.2.3.38: alpha-bisabolene 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 MG A D566 D570 D529 D533
BS02 MG A D713 T717 E721 D676 T680 E684
BS03 MG A D566 D570 D529 D533
BS04 GST A R529 R531 D566 R710 K800 R492 R494 D529 R673 K763
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0010333 terpene synthase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
GO:0052681 alpha-bisabolene synthase activity
Biological Process
GO:0008299 isoprenoid biosynthetic process
GO:0016102 diterpenoid 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:3sdu, PDBe:3sdu, PDBj:3sdu
PDBsum3sdu
PubMed22153510
UniProtO81086|TPSD1_ABIGR Alpha-bisabolene synthase (Gene Name=ag1)

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