Structure of PDB 1yyr Chain B

Receptor sequence
>1yyrB (length=352) Species: 5514 (Fusarium sporotrichioides) [Search protein sequence]
NFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPRQ
QQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDDS
KDDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLIR
STLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQFN
ERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVSDE
ISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHLCD
RRFRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQLA
NV
3D structure
PDB1yyr Molecular Recognition of the Substrate Diphosphate Group Governs Product Diversity in Trichodiene Synthase Mutants.
ChainB
Resolution2.5 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) Y91 T94 L95 D98 R180 K230 R302 F303
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 N223 S227 E231
BS02 SAZ B M73 W78 T96 L97 G186 V191 M221 Y295 M71 W76 T94 L95 G184 V189 M219 Y293 PDBbind-CN: -logKd/Ki=6.29,Ki=0.51uM
BS03 POP B D100 R182 N225 S229 K232 E233 R304 F305 D98 R180 N223 S227 K230 E231 R302 F303
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:1yyr, PDBe:1yyr, PDBj:1yyr
PDBsum1yyr
PubMed15835903
UniProtP13513|TRI5_FUSSP Trichodiene synthase (Gene Name=TRI5)

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