Structure of PDB 3ctl Chain A

Receptor sequence

>3ctlA (length=219) Species: 562 (Escherichia coli)

MKISPSLMCMDLLKFKEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVS
QVKKLATKPLDCHLMVTRPQDYIAQLARAGADFITLHPETINGQAFRLID
EIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEM
LDKLAELKAWREREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGTSGLF
NHAENIDEAWRIMTAQILA

3D structure

• PDB: 3ctl Structural basis for substrate specificity in phosphate binding (beta/alpha)8-barrels: D-allulose 6-phosphate 3-epimerase from Escherichia coli K-12.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S6 H30 D32 M34 H63 M65 M135 D173
• Catalytic site (residue number reindexed from 1): S6 H30 D32 M34 H63 M65 M135 D173
• Enzyme Commision number: 5.1.3.-

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	S6P	A	S6 M8 H30 D32 H63 M65 A142 D173 G174 S175 S197	S6 M8 H30 D32 H63 M65 A142 D173 G174 S175 S197
BS02	MG	A	H30 D32 H63 D173	H30 D32 H63 D173

Gene Ontology

Molecular Function

• GO:0004750 D-ribulose-phosphate 3-epimerase activity
• GO:0016853 isomerase activity
• GO:0016857 racemase and epimerase activity, acting on carbohydrates and derivatives
• GO:0034700 allulose 6-phosphate 3-epimerase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0009052 pentose-phosphate shunt, non-oxidative branch
• GO:0019316 D-allose catabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:3ctl, PDBe:3ctl, PDBj:3ctl
• PDBsum: 3ctl
• PubMed: 18700786
• UniProt: P32719|ALSE_ECOLI D-allulose-6-phosphate 3-epimerase (Gene Name=alsE)