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protein ligands metals links
Lyase PDB id
1hxa
Jmol
Contents
Protein chain
528 a.a. *
Ligands
FHP
Metals
_MG ×3
Waters ×209
* Residue conservation analysis
PDB id:
1hxa
Name: Lyase
Title: Crystal structure of teas w273s form 2
Structure: 5-epi-aristolochene synthase. Chain: a. Synonym: teas. Engineered: yes. Mutation: yes
Source: Nicotiana tabacum. Common tobacco. Organism_taxid: 4097. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.32Å     R-factor:   0.225     R-free:   0.246
Authors: C.S.Starks,K.A.Rising,J.Chappell,J.P.Noel
Key ref: C.S.Starks et al. Single active site mutations change the specificity of a sesquiterpene cyclase. To be published,
Date:
12-Jan-01     Release date:   24-Jun-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q40577  (5EAS_TOBAC) -  5-epi-aristolochene synthase
Seq:
Struc:
 
Seq:
Struc:
548 a.a.
528 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.4.2.3.61  - 5-epiaristolochene synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (2E,6E)-farnesyl diphosphate = +-5-epiaristolochene + diphosphate
(2E,6E)-farnesyl diphosphate
= (+)-5-epiaristolochene
Bound ligand (Het Group name = FHP)
matches with 66.67% similarity
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     metabolic process   1 term 
  Biochemical function     lyase activity     4 terms