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PDBsum entry 1o5k

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protein metals Protein-protein interface(s) links
Lyase PDB id
1o5k
Jmol
Contents
Protein chains
295 a.a. *
Metals
_CA
Waters ×508
* Residue conservation analysis
PDB id:
1o5k
Name: Lyase
Title: Crystal structure of dihydrodipicolinate synthase (tm1521) f thermotoga maritima at 1.80 a resolution
Structure: Dihydrodipicolinate synthase. Chain: a, b. Synonym: dhdps. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm1521. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.80Å     R-factor:   0.142     R-free:   0.186
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref: Joint center for structural genomics (jcsg) Crystal structure of dihydrodipicolinate synthase (tm1521) from thermotoga maritima at 1.80 a resolution. To be published, .
Date:
22-Sep-03     Release date:   07-Oct-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9X1K9  (DAPA_THEMA) -  4-hydroxy-tetrahydrodipicolinate synthase
Seq:
Struc:
294 a.a.
295 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.4.3.3.7  - 4-hydroxy-tetrahydrodipicolinate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5- tetrahydro-(2S)-dipicolinate + H2O
Pyruvate
+ L-aspartate-4-semialdehyde
= (4S)-4-hydroxy-2,3,4,5- tetrahydro-(2S)-dipicolinate
+ H(2)O
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   5 terms 
  Biochemical function     catalytic activity     4 terms