Structure of PDB 1jdi Chain E

Receptor sequence

>1jdiE (length=223) Species: 83333 (Escherichia coli K-12)

MLEDLKRQVLEANLALPKHNLVTLTWGNVSAVDRERGVFVIKPSGVDYSI
MTADDMVVVSIETGEVVEGAKKPSSDTPTHRLLYQAFPSIGGIVHTHSRH
ATIWAQAGQSIPATGTTHADYFYGTIPCTRKMTDAEINGEYEWETGNVIV
ETFEKQGIDAAQMPGVLVHSHGPFAWGKNAEDAVHNAIVLEEVAYMGIFC
RQLAPQLPDMQQTLLNKHYLRKH

3D structure

• PDB: 1jdi The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
• Chain: E
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D76 H95 H97 T116 D120 H171
• Catalytic site (residue number reindexed from 1): D76 H95 H97 T116 D120 H171
• Enzyme Commision number: 5.1.3.4: L-ribulose-5-phosphate 4-epimerase.

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	ZN	E	H95 H97 H171	H95 H97 H171

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0008270 zinc ion binding
• GO:0008742 L-ribulose-phosphate 4-epimerase activity
• GO:0016832 aldehyde-lyase activity
• GO:0016853 isomerase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0005996 monosaccharide metabolic process
• GO:0019323 pentose catabolic process
• GO:0019324 L-lyxose metabolic process
• GO:0019568 arabinose catabolic process
• GO:0019569 L-arabinose catabolic process to xylulose 5-phosphate
• GO:0019572 L-arabinose catabolic process

Cellular Component

• GO:0005829 cytosol
• GO:0032991 protein-containing complex

External links

• PDB: RCSB:1jdi, PDBe:1jdi, PDBj:1jdi
• PDBsum: 1jdi
• PubMed: 11732895
• UniProt: P08203|ARAD_ECOLI L-ribulose-5-phosphate 4-epimerase AraD (Gene Name=araD)