Structure of PDB 2q9z Chain B

Receptor sequence
>2q9zB (length=353) Species: 5514 (Fusarium sporotrichioides) [Search protein sequence]
ENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPR
QQQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDD
SKDDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLI
RSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQF
NERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVSD
EISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHLC
DRRYRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQL
ANV
3D structure
PDB2q9z Exploring biosynthetic diversity with trichodiene synthase.
ChainB
Resolution2.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y93 T96 L97 D100 R182 K232 R304 Y305
Catalytic site (residue number reindexed from 1) Y92 T95 L96 D99 R181 K231 R303 Y304
Enzyme Commision number 4.2.3.6: trichodiene 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 B N225 E233 N224 E232
BS02 MG B D100 D239 D99 D238
BS03 MG B D100 N185 D99 N184
BS04 POP B D100 R182 N225 K232 E233 R304 Y305 D99 R181 N224 K231 E232 R303 Y304
Gene Ontology
Molecular Function
GO:0016829 lyase activity
GO:0016838 carbon-oxygen lyase activity, acting on phosphates
GO:0045482 trichodiene synthase activity
GO:0046872 metal ion binding
Biological Process
GO:0016106 sesquiterpenoid biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2q9z, PDBe:2q9z, PDBj:2q9z
PDBsum2q9z
PubMed17678871
UniProtP13513|TRI5_FUSSP Trichodiene synthase (Gene Name=TRI5)

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