Structure of PDB 2ps8 Chain B

Receptor sequence

>2ps8B (length=354) Species: 5514 (Fusarium sporotrichioides)

MENFPTEYFLNTTVRLLEYIRYRDSNYTREERIENLHYAYNKAAHHFAQP
RQQQLLKVDPKRLQASLQTIVGMVVYSWAKVSKECMADLSIHYTYTLVLD
DSKDDPYPTMVNYFDDLQAGREQAHPWWALVNEHFPNVLRHFGPFCSLNL
IRSTLDFFEGCWIEQYNFGGFPGSHDYPQFLRRMNGLGHCVGASLWPKEQ
FNERSLFLEITSAIAQMENWMVWVNDLMSFYKEFDDERDQISLVKNYVVS
DEISLHEALEKLTQDTLHSSKQMVAVFSDKDPQVMDTIECFMHGFVTWHL
CDRRYRLSEIYEKVKEEKTEDAQKFCKFYEQAANVGAVSPSEWAYPPVAQ
LANV

3D structure

• PDB: 2ps8 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.
• Chain: B
• Resolution: 2.67 Å

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	B	N225 S229 E233	N225 S229 E233
BS02	MG	B	D100 E164	D100 E164
BS03	POP	B	D100 R182 N225 S229 K232 E233 R304 Y305	D100 R182 N225 S229 K232 E233 R304 Y305

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

External links

• PDB: RCSB:2ps8, PDBe:2ps8, PDBj:2ps8
• PDBsum: 2ps8
• PubMed: 17996718
• UniProt: P13513|TRI5_FUSSP Trichodiene synthase (Gene Name=TRI5)