Structure of PDB 2r8o Chain A

Receptor sequence
>2r8oA (length=662) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SSRKELANAIRALSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLKHNPQN
PSWADRDRFVLSNGHGSMLIYSLLHLTGYDLPMEELKNFRQLHSKTPGHP
EVGYTAGVETTTGPLGQGIANAVGMAIAEKTLAAQFNRPGHDIVDHYTYA
FMGDGCMMEGISHEVCSLAGTLKLGKLIAFYDDNGISIDGHVEGWFTDDT
AMRFEAYGWHVIRDIDGHDAASIKRAVEEARAVTDKPSLLMCKTIIGFGS
PNKAGTHDSHGAPLGDAEIALTREQLGWKYAPFEIPSEIYAQWDAKEAGQ
AKESAWNEKFAAYAKAYPQEAAEFTRRMKGEMPSDFDAKAKEFIAKLQAN
PAKIASRKASQNAIEAFGPLLPEFLGGSADLAPSNLTLWSGSKAINEDAA
GNYIHYGVREFGMTAIANGISLHGGFLPYTSTFLMFVEYARNAVRMAALM
KQRQVMVYTHDSIGLGEDGPTHQPVEQVASLRVTPNMSTWRPCDQVESAV
AWKYGVERQDGPTALILSRQNLAQQERTEEQLANIARGGYVLKDCAGQPE
LIFIATGSEVELAVAAYEKLTAEGVKARVVSMPSTDAFDKQDAAYRESVL
PKAVTARVAVEAGIADYWYKYVGLNGAIVGMTTFGESAPAELLFEEFGFT
VDNVVAKAKELL
3D structure
PDB2r8o Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate.
ChainA
Resolution1.47 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H26 I247 H261 E411 H473
Catalytic site (residue number reindexed from 1) H25 I246 H260 E410 H472
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 CA A D155 N185 I187 D154 N184 I186
BS02 T5X A H26 H66 H100 G114 L116 D155 G156 N185 I187 I189 I247 H261 H25 H65 H99 G113 L115 D154 G155 N184 I186 I188 I246 H260
BS03 T5X A D381 S385 E411 F434 F437 Y440 H461 D469 H473 R520 D380 S384 E410 F433 F436 Y439 H460 D468 H472 R519
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004802 transketolase activity
GO:0016740 transferase activity
GO:0030145 manganese ion binding
GO:0030976 thiamine pyrophosphate binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006098 pentose-phosphate shunt
GO:0009052 pentose-phosphate shunt, non-oxidative branch
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2r8o, PDBe:2r8o, PDBj:2r8o
PDBsum2r8o
PubMed17914867
UniProtP27302|TKT1_ECOLI Transketolase 1 (Gene Name=tktA)

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