Structure of PDB 4f2d Chain C

Receptor sequence
>4f2dC (length=498) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MTIFDNYEVWFVIGSQHLYGPETLRQVTQHAEHVVNALNTEAKLPCKLVL
KPLGTTPDEITAICRDANYDDRCAGLVVWLHTFSPAKMWINGLTMLNKPL
LQFHTQFNAALPWDSIDMDFMNLNQTAHGGREFGFIGARMRQQHAVVTGH
WQDKQAHERIGSWMRQAVSKQDTRHLKVCRFGDNMREVAVTDGDKVAAQI
KFGFSVNTWAVGDLVQVVNSISDGDVNALVDEYESCYTMTPATQIHGEKR
QNVLEAARIELGMKRFLEQGGFHAFTTTFEDLHGLKQLPGLAVQRLMQQG
YGFAGEGDWKTAALLRIMKVMSTGLQGGTSFMEDYTYHFEKGNDLVLGSH
MLEVCPSIAVEEKPILDVQHLGIGGKDDPARLIFNTQTGPAIVASLIDLG
DRYRLLVNCIDTVKTPHSLPKLPVANALWKAQPDLPTASEAWILAGGAHH
TVFSHALNLNDMRQFAEMHDIEITVIDNDTRLPAFKDALRWNEVYYGF
3D structure
PDB4f2d Crystal Structure of Escherichia coli L-arabinose Isomerase (ECAI) complexed with Ribitol
ChainC
Resolution2.3 Å
3D
structure
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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 C E306 E333 H350 H450 E306 E333 H350 H450
BS02 RB0 C M185 F279 E306 E333 H449 M185 F279 E306 E333 H449
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4f2d, PDBe:4f2d, PDBj:4f2d
PDBsum4f2d
PubMed
UniProtP08202|ARAA_ECOLI L-arabinose isomerase (Gene Name=araA)

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