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PDBsum entry 2pcq

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protein ligands metals links
Lyase PDB id
2pcq
Jmol PyMol
Contents
Protein chain
283 a.a. *
Ligands
GOL ×2
Metals
__K
Waters ×440
* Residue conservation analysis
PDB id:
2pcq
Name: Lyase
Title: Crystal structure of putative dihydrodipicolinate synthase ( from thermus thermophilus hb8
Structure: Putative dihydrodipicolinate synthase. Chain: a. Engineered: yes
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.164     R-free:   0.193
Authors: J.Jeyakanthan,S.P.Kanaujia,C.Vasuki Ranjani,K.Sekar,Y.Kitamu A.Ebihara,S.Kuramitsu,A.Shinkai,Y.Shiro,S.Yokoyama,Riken St Genomics/proteomics Initiative (Rsgi)
Key ref: J.Jeyakanthan et al. Crystal structure of putative dihidrodipicolinate synthase (ttha0737) from thermus thermophilus hb8. To be published, .
Date:
30-Mar-07     Release date:   02-Oct-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q5SKB1  (Q5SKB1_THET8) -  Putative dihidrodipicolinate synthase
Seq:
Struc:
283 a.a.
283 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.2.1.52  - Transferred entry: 4.3.3.7.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Lysine biosynthesis (early stages)
      Reaction: L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H2O
L-aspartate 4-semialdehyde
+
pyruvate
Bound ligand (Het Group name = GOL)
matches with 71.43% similarity
= dihydrodipicolinate
+ 2 × H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     lyase activity     1 term  

 

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