PDBsum entry 1qzu

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protein ligands links
Lyase PDB id
Protein chain
160 a.a. *
FMN ×4
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Crystal structure of human phosphopantothenoylcysteine decar
Structure: Hypothetical protein mds018. Chain: a, b, c, d. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: coac. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Trimer (from PDB file)
2.91Å     R-factor:   0.293     R-free:   0.342
Authors: N.Manoj,S.E.Ealick
Key ref:
N.Manoj and S.E.Ealick (2003). Unusual space-group pseudosymmetry in crystals of human phosphopantothenoylcysteine decarboxylase. Acta Crystallogr D Biol Crystallogr, 59, 1762-1766. PubMed id: 14501115 DOI: 10.1107/S0907444903016214
17-Sep-03     Release date:   23-Mar-04    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q96CD2  (COAC_HUMAN) -  Phosphopantothenoylcysteine decarboxylase
204 a.a.
160 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.  - Phosphopantothenoylcysteine decarboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Coenzyme A Biosynthesis (late stages)
      Reaction: N-((R)-4'-phosphopantothenoyl)-L-cysteine = pantotheine 4'-phosphate + CO2
= pantotheine 4'-phosphate
+ CO(2)
      Cofactor: FMN
Bound ligand (Het Group name = FMN) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytosol   1 term 
  Biological process     small molecule metabolic process   6 terms 
  Biochemical function     catalytic activity     4 terms  


    Added reference    
DOI no: 10.1107/S0907444903016214 Acta Crystallogr D Biol Crystallogr 59:1762-1766 (2003)
PubMed id: 14501115  
Unusual space-group pseudosymmetry in crystals of human phosphopantothenoylcysteine decarboxylase.
N.Manoj, S.E.Ealick.
Phosphopantothenoylcysteine (PPC) decarboxylase is an essential enzyme in the biosynthesis of coenzyme A and catalyzes the decarboxylation of PPC to phosphopantetheine. Human PPC decarboxylase has been expressed in Escherichia coli, purified and crystallized. The Laue class of the diffraction data appears to be 3m, suggesting space group R32 with two monomers per asymmetric unit. However, the crystals belong to the space group R3 and the asymmetric unit contains four monomers. The structure has been solved using molecular replacement and refined to a current R factor of 29%. The crystal packing can be considered as two interlaced lattices, each consistent with space group R32 and with the corresponding twofold axes parallel to each other but separated along the threefold axis. Thus, the true space group is R3 with four monomers per asymmetric unit.
  Selected figure(s)  
Figure 2.
Figure 2 Stereoview showing electron density for PPC decarboxylase. (a) F[o] - F[c] map contoured at 1.8 showing the location of the bound FMN. The FMN molecule was not included in the refinement or in the calculated phases. (b) Section from a 2F[o] - F[c] composite omit map. The density corresponds to a helix-turn-helix region and is contoured at 1.0 . This figure was created using BOBSCRIPT (Esnouf, 1999[Esnouf, R. M. (1999). Acta Cryst. D55, 938-940.]) and Raster3D (Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 1762-1766) copyright 2003.  
  Figure was selected by an automated process.