Structure of PDB 2r5n Chain B

Receptor sequence
>2r5nB (length=663) Species: 562 (Escherichia coli) [Search protein sequence]
SSRKELANAIRALSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLKHNPQN
PSWADRDRFVLSNGHGSMLIYSLLHLTGYDLPMEELKNFRQLHSKTPGHP
EVGYTAGVETTTGPLGQGIANAVGMAIAEKTLAAQFNRPGHDIVDHYTYA
FMGDGCMMEGISHEVCSLAGTLKLGKLIAFYDDNGISIDGHVEGWFTDDT
AMRFEAYGWHVIRDIDGHDAASIKRAVEEARAVTDKPSLLMCKTIIGFGS
PNKAGTHDSHGAPLGDAEIALTREQLGWKYAPFEIPSEIYAQWDAKEAGQ
AKESAWNEKFAAYAKAYPQEAAEFTRRMKGEMPSDFDAKAKEFIAKLQAN
PAKIASRKASQNAIEAFGPLLPEFLGGSADLAPSNLTLWSGSKAINEDAA
GNYIHYGVREFGMTAIANGISLHGGFLPYTSTFLMFVEYARNAVRMAALM
KQRQVMVYTHDSIGLGEDGPTHQPVEQVASLRVTPNMSTWRPCDQVESAV
AWKYGVERQDGPTALILSRQNLAQQERTEEQLANIARGGYVLKDCAGQPE
LIFIATGSEVELAVAAYEKLTAEGVKARVVSMPSTDAFDKQDAAYRESVL
PKAVTARVAVEAGIADYWYKYVGLNGAIVGMTTFGESAPAELLFEEFGFT
VDNVVAKAKELLH
3D structure
PDB2r5n 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.
ChainB
Resolution1.6 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) 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 R5P B H26 H261 H25 H260
BS02 TPP B D381 E411 F437 Y440 D380 E410 F436 Y439
BS03 CA B D155 N185 I187 D154 N184 I186
BS04 RP5 B H26 I189 H261 H25 I188 H260
BS05 TPP B H66 G114 L116 D155 G156 N185 I187 I189 I247 H261 H65 G113 L115 D154 G155 N184 I186 I188 I246 H260
BS06 RP5 B S385 H461 D469 R520 S384 H460 D468 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2r5n, PDBe:2r5n, PDBj:2r5n
PDBsum2r5n
PubMed17914867
UniProtP27302|TKT1_ECOLI Transketolase 1 (Gene Name=tktA)

[Back to BioLiP]