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Ligands
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Glycosylation
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PYR Pyruvic acid
Code : 1AW8   PDBj   RCSB PDB   PDBe
Header : DECARBOXYLASE
Title : PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE
Release Data : 1998-04-29
Compound :
mol_id molecule chains
1 L-ASPARTATE-ALPHA-DECARBOXYLASE A,D
ec: 4.1.1.11
mol_id molecule chains
2 L-ASPARTATE-ALPHA-DECARBOXYLASE B,E
ec: 4.1.1.11
other_details: microheterogeneity at residue B25
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
mol_id organism_scientific expression_system
2 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
Authors : Albert, A., Dhanaraj, V., Genschel, U., Khan, G., Ramjee, M.K., Pulido, R., Sybanda, B.L., von Delf, F., Witty, M., Blundell, T.L., Smith, A.G., Abell, C.
Keywords : DECARBOXYLASE, PANTOTHENATE PATHWAY, LYASE, PROTEIN SELF-PROCESSING
Exp. method : X-RAY DIFFRACTION ( 2.2 Å )
Citation :

Crystal structure of aspartate decarboxylase at 2.2 A 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

PubMed: 9546220
DOI: 10.1038/nsb0498-289

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