Structure of PDB 2hxg Chain A

Receptor sequence

>2hxgA (length=498) Species: 562 (Escherichia coli)

MTIFDNYEVWFVIGSQHLYGPETLRQVTQHAEHVVNALNTEAKLPCKLVL
KPLGTTPDEITAICRDANYDDPCAGLVVWLHTFSPAKMWINGLTMLNKPL
LQFHTQFNAALPWDSIDMDFMNLNQTAHGGREFGFIGARMRQQHAVVTGH
WQDKQAHERIGSWMRQAVSKQDTRHLKVCRFGDNMREVAVTDGDKVAAQI
KFGFSVNTWAVGDLVQVVNSISDGDVNALVDEYESCYTMTPATQIHGEKR
QNVLEAARIELGMKRFLEQGGFHAFTTTFEDLHGLKQLPGLAVQRLMQQG
YGFAGEGDWKTAALLRIMKVMSTGLQGGTSFMEDYTYHFEKGNDLVLGSH
MLEVCPSIAVEEKPILDVQHLGIGGKDDPARLIFNTQTGPAIVASLIDLG
DRYRLLVNCIDTVKTPHSLPKLPVANALWKAQPDLPTASEAWILAGGAHH
TVFSHALNLNDMRQFAEMHDIEITVIDNDTRLPAFKDALRWNEVYYGF

3D structure

• PDB: 2hxg Crystal Structure of Mn2+-bound Escherichia coli L-arabinose Isomerase (ECAI) and Implications in Protein Catalytic Mechanism and Thermo-Stability.
• Chain: A
• Resolution: 2.8 Å

Enzymatic activity

• Enzyme Commision number: 5.3.1.4: L-arabinose isomerase.

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	MN	A	E306 E333 H350 H450	E306 E333 H350 H450

Gene Ontology

Molecular Function

• GO:0008733 L-arabinose isomerase activity
• GO:0016853 isomerase activity
• GO:0016861 intramolecular oxidoreductase activity, interconverting aldoses and ketoses
• GO:0030145 manganese ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0005996 monosaccharide metabolic process
• GO:0019568 arabinose catabolic process
• GO:0019569 L-arabinose catabolic process to xylulose 5-phosphate

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:2hxg, PDBe:2hxg, PDBj:2hxg
• PDBsum: 2hxg
• UniProt: P08202|ARAA_ECOLI L-arabinose isomerase (Gene Name=araA)