Structure of PDB 1yyt Chain B

Receptor sequence
>1yytB (length=354) Species: 5514 (Fusarium sporotrichioides) [Search protein sequence]
MENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQP
RQQQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLE
DSKDDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNL
IRSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQ
FNERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVS
DEISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHL
CDRRYRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQ
LANV
3D structure
PDB1yyt Molecular Recognition of the Substrate Diphosphate Group Governs Product Diversity in Trichodiene Synthase Mutants.
ChainB
Resolution2.9 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 E100 R182 K232 R304 Y305
Catalytic site (residue number reindexed from 1) Y93 T96 L97 E100 R182 K232 R304 Y305
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 POP B R182 N225 Y305 R182 N225 Y305
BS02 SAZ B T96 L97 G186 L187 M221 N225 Y295 W298 T96 L97 G186 L187 M221 N225 Y295 W298
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
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Biological Process
External links
PDB RCSB:1yyt, PDBe:1yyt, PDBj:1yyt
PDBsum1yyt
PubMed15835903
UniProtP13513|TRI5_FUSSP Trichodiene synthase (Gene Name=TRI5)

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