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Ligands
Code Name Style Show Link
LI Lithium ion
MES 2-(N-morpholino)-ethanesulfonic acid
NA Sodium ion
PLP Pyridoxal-5'-phosphate
Non-standard Residues
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Glycosylation
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Code : 1DGD   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : AN ALKALI METAL ION SIZE-DEPENDENT SWITCH IN THE ACTIVE SITE STRUCTURE OF DIALKYLGLYCINE DECARBOXYLASE
Release Data : 1994-09-30
Compound :
mol_id molecule chains
1 DIALKYLGLYCINE DECARBOXYLASE A
ec: 4.1.1.64
Source :
mol_id organism_scientific
1 Burkholderia cepacia  (taxid:292)
Authors : Hohenester, E., Jansonius, J.N.
Keywords : LYASE
Exp. method : X-RAY DIFFRACTION ( 2.8 Å )
Citation :

An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase.

Hohenester, E.,Keller, J.W.,Jansonius, J.N.
(1994)  Biochemistry  33 : 13561 - 13570

PubMed: 7947767
DOI: 10.1021/bi00250a008

Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Sites

Toney, M.D.,Hohenester, E.,Jacob, S.W.  et al.
(1993)  Science  261 : 756

Pseudomonas Cepacia 2,2-Dialkylglycine Decarboxylase. Sequence and Expression in Escherichia Coli of Structural and Repressor Genes

Keller, J.W.,Baurick, K.B.,Rutt, G.C.  et al.
(1990)  J.Biol.Chem.  265 : 5531

Chain : A
UniProt : P16932 (DGDA_BURCE)
Reaction: EC: Evidence:
Physiological Direction:
2,2-dialkylglycine + H(+) + pyruvate = CO2 + dialkyl ketone + L-alanine 4.1.1.64 -
-