7A8Y | pdb_00007a8y

X-ray crystal structure of Aspartate alpha-decarboxylase in complex with D-Serine


Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
A [auth AAA]Asp_decarboxe7a8yAAA1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Asp_decarboxECOD (1.6)
C [auth DDD]Asp_decarboxe7a8yDDD1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Asp_decarboxECOD (1.6)
B [auth BBB]Asp_decarboxe7a8yBBB1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Asp_decarboxECOD (1.6)
D [auth EaE]Asp_decarboxe7a8yEaE1 A: beta barrelsX: cradle loop barrelH: RIFT-relatedT: double psiF: Asp_decarboxECOD (1.6)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
B [auth BBB],
D [auth EaE]
PF02261Aspartate decarboxylase (Asp_decarbox)Aspartate decarboxylaseDecarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalysed by the enzyme aspartate decarboxylase EC:4.1.1.11 which requires a pyruvoyl group for its activity. It is synthesised initially as a proenzyme wh ...Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A [auth AAA],
C [auth DDD]
Aspartate 1-decarboxylase
B [auth BBB],
D [auth EaE]
Aspartate 1-decarboxylase

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
B [auth BBB],
D [auth EaE]
PYR RESIDAA0127

PSI-MOD :  pyruvic acid (Cys) MOD:00136 , pyruvic acid (Ser) MOD:00807 , pyruvic acid MOD:01154 , pyruvic acid (Tyr) MOD:01661