Structure of PDB 1dxf Chain A

Receptor sequence

>1dxfA (length=253) Species: 562 (Escherichia coli)

DVFPNKFKAALAAKQVQIGCWSALSNPISTEVLGLAGFDWLVLDGEHAPN
DISTFIPQLMALKGSASAPVVRVPTNEPVIIKRLLDIGFYNFLIPFVETK
EEAELAVASTRYPPEGIRGVSVSHRANMFGTVADYFAQSNKNITILVQIE
SQQGVDNVDAIAATEGVDGIFVGPSDLAAALGHLGNASHPDVQKAIQHIF
NRASAHGKPSGILAPVEADARRYLEWGATFVAVGSDLGVFRSATQKLADT
FKK

3D structure

• PDB: 1dxf Crystal Structures of the Metal-Dependent 2-Dehydro-3-Deoxy-Galactarate Aldolase Suggest a Novel Reaction Mechanism.
• Chain: A
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H50 R75 D89 E153 D179
• Catalytic site (residue number reindexed from 1): H47 R72 D86 E150 D176
• Enzyme Commision number: 4.1.2.20: 2-dehydro-3-deoxyglucarate 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	E153 G176 P177 S178 D179	E150 G173 P174 S175 D176
BS02	MG	A	E153 D179	E150 D176

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0008672 2-dehydro-3-deoxyglucarate aldolase activity
• GO:0016829 lyase activity
• GO:0016830 carbon-carbon lyase activity
• GO:0016832 aldehyde-lyase activity
• GO:0046872 metal ion binding
• GO:0061677 2-dehydro-3-deoxy-D-gluconate aldolase activity

Biological Process

• GO:0019394 glucarate catabolic process
• GO:0042838 D-glucarate catabolic process
• GO:0046392 galactarate catabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1dxf, PDBe:1dxf, PDBj:1dxf
• PDBsum: 1dxf
• PubMed: 10921867
• UniProt: P23522|GARL_ECOLI 5-keto-4-deoxy-D-glucarate aldolase (Gene Name=garL)