Structure of PDB 2ps7 Chain A

Receptor sequence
>2ps7A (length=354) Species: 5514 (Fusarium sporotrichioides) [Search protein sequence]
MENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQP
RQQQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLD
DSKDDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNL
IRSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQ
FNERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVS
DEISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGFVTWHL
CDRRYRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQ
LANV
3D structure
PDB2ps7 Structural and mechanistic analysis of trichodiene synthase using site-directed mutagenesis: probing the catalytic function of tyrosine-295 and the asparagine-225/serine-229/glutamate-233-Mg2+B motif.
ChainA
Resolution2.35 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) Y93 T96 L97 D100 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 MG A D239 I241 D239 I241
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:2ps7, PDBe:2ps7, PDBj:2ps7
PDBsum2ps7
PubMed17996718
UniProtP13513|TRI5_FUSSP Trichodiene synthase (Gene Name=TRI5)

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