Structure of PDB 3ct7 Chain E

Receptor sequence
>3ct7E (length=219) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MKISPSLMCMDLLKFKEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVS
QVKKLATKPLDCHLMVTRPQDYIAQLARAGADFITLHPETINGQAFRLID
EIRRHDMKVGLILNPETPVEAMKYYIHKADKITVMTVDPGFAGQPFIPEM
LDKLAELKAWREREGLEYEIEVDGSCNQATYEKLMAAGADVFIVGTSGLF
NHAENIDEAWRIMTAQILA
3D structure
PDB3ct7 Structural basis for substrate specificity in phosphate binding (beta/alpha)8-barrels: D-allulose 6-phosphate 3-epimerase from Escherichia coli K-12.
ChainE
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MG E 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3ct7, PDBe:3ct7, PDBj:3ct7
PDBsum3ct7
PubMed18700786
UniProtP32719|ALSE_ECOLI D-allulose-6-phosphate 3-epimerase (Gene Name=alsE)

[Back to BioLiP]