Brand  (β version)

PDB ID: 1PPY

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
SO4 Sulfate ion PoSSuM
Non-standard Residues
Code Name Show
CSX S-oxy cysteine
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1PPY   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : Native precursor of pyruvoyl dependent Aspartate decarboxylase
Release Data : 2003-11-18
Compound :
mol_id molecule chains synonym
1 Aspartate 1-decarboxylase precursor A,B Aspartate alpha-decarboxylase precursor
ec: 4.1.1.11
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
gene: PAND OR B0131 OR C0160 OR Z0142 OR ECS0135 OR SF0128
expression_system_strain: SJ16
expression_system_plasmid: pBluescript KS
Authors : Schmitzberger, F., Kilkenny, M.L., Lobley, C.M.C., Webb, M.E., Vinkovic, M., Matak-Vinkovic, D., Witty, M., Chirgadze, D.Y., Smith, A.G., Abell, C., Blundell, T.L.
Keywords : decarboxylase, pantothenate pathway, intramolecular protein self-processing, LYASE
Exp. method : X-RAY DIFFRACTION ( 1.95 Å )
Citation :

Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase

Schmitzberger, F.,Kilkenny, M.L.,Lobley, C.M.C.  et al.
(2003)  Embo J.  22 : 6193 - 6204

PubMed: 14633979
DOI: 10.1093/emboj/cdg575

Purification and properties of L-Aspartate-alpha-decarboxylase, an enzyme that catalyzes the formation of beta-alanine in Escherichia coli

Williamson, J.M.,Brown, G.M.
(1979)  J.Biol.Chem.  254 : 8074 - 8082

Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry

Ramjee, M.K.,Genschel, U.,Abell, C.  et al.
(1997)  Biochem.J.  323 : 661 - 669

Crystal structure of aspartate decarboxylase at 2.2A resolution provides evidence for an ester in protein self-processing

Albert, A.,Dhanaraj, V.,Genschel, U.  et al.
(1998)  Nat.Struct.Biol.  5 : 289 - 293

Reaction

Chain : A, B
UniProt : P0A790 (PAND_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
H(+) + L-aspartate = beta-alanine + CO2 4.1.1.11 PubMed:6767707
-