Structure of PDB 4xz9 Chain B

Receptor sequence
>4xz9B (length=217) Species: 273075 (Thermoplasma acidophilum DSM 1728) [Search protein sequence]
MKIFLDTANIDEIRTGVNWGIVDGVTTNPTLISKEAVNGKKYGDIIREIL
KIVDGPVSVQVVSTKYEGMVEEARKIHGLGDNAVVKIPMTEDGLRAIKTL
SSEHINTNCTLVFNPIQALLAAKAGVTYVSPYVGRLDDIGEDGMQIIDMI
RTIFNNYIIKTQILVASIRNPIHVLRSAVIGADVVTVPFNVLKSLMKHPK
TDEGLAKFLEDWKKVSP
3D structure
PDB4xz9 Converting Transaldolase into Aldolase through Swapping of the Multifunctional Acid-Base Catalyst: Common and Divergent Catalytic Principles in F6P Aldolase and Transaldolase.
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D6 Q60 K86 T110 Y132
Catalytic site (residue number reindexed from 1) D6 Q60 K86 T110 Y132
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 PDO B D6 T26 N28 K86 S130 D6 T26 N28 K86 S130
BS02 G3P B D6 R135 S167 R169 D6 R135 S167 R169
Gene Ontology
Molecular Function
GO:0004801 transaldolase activity
GO:0016740 transferase activity
GO:0016832 aldehyde-lyase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006098 pentose-phosphate shunt
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4xz9, PDBe:4xz9, PDBj:4xz9
PDBsum4xz9
PubMed26131847
UniProtQ9HKI3|TAL_THEAC Probable transaldolase (Gene Name=tal)

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