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PDBsum entry 1ko0

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protein ligands links
Lyase PDB id
1ko0
Jmol
Contents
Protein chain
419 a.a. *
Ligands
PLP-LYS
DLY
Waters ×384
* Residue conservation analysis
PDB id:
1ko0
Name: Lyase
Title: Crystal structure of a d,l-lysine complex of diaminopimelate decarboxylase
Structure: Diaminopimelate decarboxylase. Chain: a. Synonym: dap decarboxylase. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: lysa. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PDB file)
Resolution:
2.20Å     R-factor:   0.181     R-free:   0.246
Authors: V.Levdikov,L.Blagova,N.Bose,C.Momany
Key ref: V.Levdikov et al. Diaminopimelate decarboxylase uses a versatile active site for stereospecific decarboxylation. To be published, .
Date:
19-Dec-01     Release date:   11-Nov-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00861  (DCDA_ECOLI) -  Diaminopimelate decarboxylase
Seq:
Struc:
420 a.a.
419 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.1.1.20  - Diaminopimelate decarboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Lysine biosynthesis (later stages)
      Reaction: Meso-2,6-diaminoheptanedioate = L-lysine + CO2
Meso-2,6-diaminoheptanedioate
=
L-lysine
Bound ligand (Het Group name = LYS)
corresponds exactly
+ CO(2)
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cellular amino acid biosynthetic process   3 terms 
  Biochemical function     catalytic activity     6 terms