Structure of PDB 1eua Chain A

Receptor sequence
>1euaA (length=213) Species: 562 (Escherichia coli) [Search protein sequence]
MKNWKTSAESILTTGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRT
ECAVDAIRAIAKEVPEAIVGAGTVLNPQQLAEVTEAGAQFAISPGLTEPL
LKAATEGTIPLIPGISTVSELMLGMDYGLKEFKFFPAEANGGVKALQAIA
GPFSQVRFCPTGGISPANYRDYLALKSVLCIGGSWLVPADALEAGDYDRI
TKLAREAVEGAKL
3D structure
PDB1eua Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E45 R49 K133
Catalytic site (residue number reindexed from 1) E45 R49 K133
Enzyme Commision number 4.1.2.14: 2-dehydro-3-deoxy-phosphogluconate aldolase.
4.1.3.16: 4-hydroxy-2-oxoglutarate aldolase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 PYR A E45 T73 I92 K133 E45 T73 I92 K133
Gene Ontology
Molecular Function
GO:0008675 2-dehydro-3-deoxy-phosphogluconate aldolase activity
GO:0008700 (R,S)-4-hydroxy-2-oxoglutarate aldolase activity
GO:0008948 oxaloacetate decarboxylase activity
GO:0016829 lyase activity
GO:0016833 oxo-acid-lyase activity
GO:0042802 identical protein binding
GO:0106009 (4S)-4-hydroxy-2-oxoglutarate aldolase activity
Biological Process
GO:0009255 Entner-Doudoroff pathway through 6-phosphogluconate
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function

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Cellular Component
External links
PDB RCSB:1eua, PDBe:1eua, PDBj:1eua
PDBsum1eua
PubMed11274385
UniProtP0A955|ALKH_ECOLI KHG/KDPG aldolase (Gene Name=eda)

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