Structure of PDB 6rjb Chain A

Receptor sequence
>6rjbA (length=620) Species: 9606 (Homo sapiens) [Search protein sequence]
ESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVL
FFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLR
KISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYC
LLGDGELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDI
YQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGV
EDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIANI
RMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIF
KKEHPDRFIECYIAEQNMVSIAVGCATRNREVPFCSTFAAFFTRAFDQIR
MAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDG
VATEKAVELAANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDD
QVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARA
TKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAEL
LKMFGIDRDAIAQAVRGLIT
3D structure
PDB6rjb Low-barrier hydrogen bonds in enzyme cooperativity.
ChainA
Resolution1.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H37 K244 H258 E366 R395 Q428
Catalytic site (residue number reindexed from 1) H36 K243 H257 E365 R394 Q427
Enzyme Commision number 2.2.1.1: transketolase.
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 TPP A S40 K75 H77 L125 G154 D155 G156 E157 N185 L187 Q189 K244 H258 S39 K74 H76 L124 G153 D154 G155 E156 N184 L186 Q188 K243 H257
BS02 MG A D155 N185 L187 D154 N184 L186
BS03 CA A D155 N185 L187 D154 N184 L186
BS04 TPP A D341 I364 E366 F392 D340 I363 E365 F391
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004802 transketolase activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0016740 transferase activity
GO:0016744 transketolase or transaldolase activity
GO:0030976 thiamine pyrophosphate binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006098 pentose-phosphate shunt
GO:0006796 phosphate-containing compound metabolic process
GO:0009052 pentose-phosphate shunt, non-oxidative branch
GO:0019637 organophosphate metabolic process
GO:0040008 regulation of growth
GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
GO:1901135 carbohydrate derivative metabolic process
GO:1901159 xylulose 5-phosphate biosynthetic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005777 peroxisome
GO:0005789 endoplasmic reticulum membrane
GO:0005829 cytosol
GO:0016604 nuclear body
GO:0031982 vesicle
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6rjb, PDBe:6rjb, PDBj:6rjb
PDBsum6rjb
PubMed31534226
UniProtP29401|TKT_HUMAN Transketolase (Gene Name=TKT)

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