Structure of PDB 2r5n Chain A

Receptor sequence

>2r5nA (length=666) Species: 562 (Escherichia coli)

SSRKELANAIRALSMDAVQKAKSGHPGAPMGMADIAEVLWRDFLKHNPQN
PSWADRDRFVLSNGHGSMLIYSLLHLTGYDLPMEELKNFRQLHSKTPGHP
EVGYTAGVETTTGPLGQGIANAVGMAIAEKTLAAQFNRPGHDIVDHYTYA
FMGDGCMMEGISHEVCSLAGTLKLGKLIAFYDDNGISIDGHVEGWFTDDT
AMRFEAYGWHVIRDIDGHDAASIKRAVEEARAVTDKPSLLMCKTIIGFGS
PNKAGTHDSHGAPLGDAEIALTREQLGWKYAPFEIPSEIYAQWDAKEAGQ
AKESAWNEKFAAYAKAYPQEAAEFTRRMKGEMPSDFDAKAKEFIAKLQAN
PAKIASRKASQNAIEAFGPLLPEFLGGSADLAPSNLTLWSGSKAINEDAA
GNYIHYGVREFGMTAIANGISLHGGFLPYTSTFLMFVEYARNAVRMAALM
KQRQVMVYTHDSIGLGEDGPTHQPVEQVASLRVTPNMSTWRPCDQVESAV
AWKYGVERQDGPTALILSRQNLAQQERTEEQLANIARGGYVLKDCAGQPE
LIFIATGSEVELAVAAYEKLTAEGVKARVVSMPSTDAFDKQDAAYRESVL
PKAVTARVAVEAGIADYWYKYVGLNGAIVGMTTFGESAPAELLFEEFGFT
VDNVVAKAKELLHHHH

3D structure

• PDB: 2r5n 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.
• Chain: A
• Resolution: 1.6 Å

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	A	S385 F434 H461 D469 H473 R520	S384 F433 H460 D468 H472 R519	MOAD: Kd=700uM
BS02	CA	A	D155 N185 I187	D154 N184 I186
BS03	TPP	A	H66 G114 L116 D155 G156 N185 I187 I189 I247 H261	H65 G113 L115 D154 G155 N184 I186 I188 I246 H260
BS04	RP5	A	S385 H461 D469 R520	S384 H460 D468 R519
BS05	TPP	A	D381 E411 F437 Y440	D380 E410 F436 Y439
BS06	RP5	A	H26 I189 H261	H25 I188 H260

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

External links

• PDB: RCSB:2r5n, PDBe:2r5n, PDBj:2r5n
• PDBsum: 2r5n
• PubMed: 17914867
• UniProt: P27302|TKT1_ECOLI Transketolase 1 (Gene Name=tktA)