Structure of PDB 4s2b Chain A

Receptor sequence
>4s2bA (length=316) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKL
IDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKLVPGRISTEVDARL
SYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGI
NCNLTLLFSFAQARACAEAGVFLISPYVGRILDWYKANTDKKEYAPAEDP
GVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPTLLKE
LAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRK
FAIDQEKLEKMIGDLL
3D structure
PDB4s2b Novel mode of inhibition by D-tagatose 6-phosphate through a Heyns rearrangement in the active site of transaldolase B variants.
ChainA
Resolution1.46 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D17 E96 K132 T156 Y178
Catalytic site (residue number reindexed from 1) D16 E95 K131 T155 Y177
Enzyme Commision number 2.2.1.2: transaldolase.
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 44S A D17 N35 K132 T156 Y178 R181 S226 R228 D16 N34 K131 T155 Y177 R180 S225 R227
Gene Ontology
Molecular Function
GO:0004801 transaldolase activity
GO:0016740 transferase activity
GO:0016744 transketolase or transaldolase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006098 pentose-phosphate shunt
GO:0009052 pentose-phosphate shunt, non-oxidative branch
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4s2b, PDBe:4s2b, PDBj:4s2b
PDBsum4s2b
PubMed27050126
UniProtP0A870|TALB_ECOLI Transaldolase B (Gene Name=talB)

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