Brand  (β version)

PDB ID: 4D9M

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Ligands
Code Name Style Show Link
0JO 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 4D9M   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : Crystal structure of Diaminopropionate ammonia lyase from Escherichia coli in complex with aminoacrylate-PLP azomethine reaction intermediate
Release Data : 2012-04-25
Compound :
mol_id molecule chains synonym
1 Diaminopropionate ammonia-lyase A,B Diaminopropionatase, Alpha,beta-diaminopropionate ammonia-lyase
ec: 4.3.1.15
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:83333) Escherichia coli  (taxid:562)
strain: K12
gene: b2871, JW2839, ygeX
expression_system_strain: BL21(DE3)pLysS
expression_system_vector_type: PLASMID
expression_system_plasmid: pRSET-C
Authors : Bisht, S., Rajaram, V., Bharath, S.R., Murthy, M.R.N.
Keywords : Fold type II PLP-dependent enzyme, Tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily, Lyase
Exp. method : X-RAY DIFFRACTION ( 2.50 Å )
Citation :

Crystal Structure of Escherichia coli Diaminopropionate Ammonia-lyase Reveals Mechanism of Enzyme Activation and Catalysis

Bisht, S.,Rajaram, V.,Bharath, S.R.  et al.
(2012)  J.Biol.Chem.  287 : 20369 - 20381

PubMed: 22505717
DOI: 10.1074/jbc.M112.351809

Reaction

Chain : A, B
UniProt : P66899 (DPAL_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
(S)-2,3-diaminopropanoate + H2O + H(+) = pyruvate + 2 NH4(+) 4.3.1.15 PubMed:12596860
-
(R)-2,3-diaminopropanoate + H2O + H(+) = pyruvate + 2 NH4(+) 4.3.1.15 PubMed:12596860
-
Cofactor: Evidence: Note:
pyridoxal 5'-phosphate ECO:0000269 | PubMed:12821154
ECO:0000269 | PubMed:22505717
Binds 1 pyridoxal phosphate per subunit.