Structure of PDB 1yyq Chain B

Receptor sequence
>1yyqB (length=351) Species: 5514 (Fusarium sporotrichioides) [Search protein sequence]
FPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQQ
QLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDSK
DDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIRS
TLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQFNE
RSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVSDEI
SLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHLCDR
RFRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQLAN
V
3D structure
PDB1yyq Molecular Recognition of the Substrate Diphosphate Group Governs Product Diversity in Trichodiene Synthase Mutants.
ChainB
Resolution2.1 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 F305
Catalytic site (residue number reindexed from 1) Y90 T93 L94 D97 R179 K229 R301 F302
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 S229 E233 N222 S226 E230
BS02 POP B D100 R182 N225 S229 K232 E233 R304 F305 D97 R179 N222 S226 K229 E230 R301 F302
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1yyq, PDBe:1yyq, PDBj:1yyq
PDBsum1yyq
PubMed15835903
UniProtP13513|TRI5_FUSSP Trichodiene synthase (Gene Name=TRI5)

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