Structure of PDB 2ps5 Chain B

Receptor sequence
>2ps5B (length=353) Species: 5514 (Fusarium sporotrichioides) [Search protein sequence]
ENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQPR
QQQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLDD
SKDDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNLI
RSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQF
NERSLFLEITSAIAQMENWMVWVDDLMSFYKEFDDERDQISLVKNYVVSD
EISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGYVTWHLC
DRRYRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQL
ANV
3D structure
PDB2ps5 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.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D225 S229 E233 D224 S228 E232
BS02 POP B D100 R182 D225 S229 K232 E233 R304 Y305 D99 R181 D224 S228 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2ps5, PDBe:2ps5, PDBj:2ps5
PDBsum2ps5
PubMed17996718
UniProtP13513|TRI5_FUSSP Trichodiene synthase (Gene Name=TRI5)

[Back to BioLiP]