Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3OOY

Crystal structure of human Transketolase (TKT)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004802	molecular_function	transketolase activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0006098	biological_process	pentose-phosphate shunt
A	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
A	0016604	cellular_component	nuclear body
A	0016607	cellular_component	nuclear speck
A	0016744	molecular_function	transketolase or transaldolase activity
A	0019682	biological_process	glyceraldehyde-3-phosphate metabolic process
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0031982	cellular_component	vesicle
A	0042803	molecular_function	protein homodimerization activity
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
A	0070062	cellular_component	extracellular exosome
A	1901159	biological_process	D-xylulose 5-phosphate biosynthetic process
B	0000287	molecular_function	magnesium ion binding
B	0004802	molecular_function	transketolase activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005777	cellular_component	peroxisome
B	0005829	cellular_component	cytosol
B	0006098	biological_process	pentose-phosphate shunt
B	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
B	0016604	cellular_component	nuclear body
B	0016607	cellular_component	nuclear speck
B	0016744	molecular_function	transketolase or transaldolase activity
B	0019682	biological_process	glyceraldehyde-3-phosphate metabolic process
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0031982	cellular_component	vesicle
B	0042803	molecular_function	protein homodimerization activity
B	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0070062	cellular_component	extracellular exosome
B	1901159	biological_process	D-xylulose 5-phosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP A 1

Chain	Residue
A	SER40
A	GLU157
A	GLU160
A	ASN185
A	LEU187
A	GLY188
A	GLN189
A	LYS244
A	HIS258
A	CA621
A	HOH627
A	LYS75
B	ASP341
B	ILE364
B	GLU366
B	PHE392
B	ARG395
B	GLN428
A	HIS77
A	GLY123
A	SER124
A	LEU125
A	GLY154
A	ASP155
A	GLY156

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 621

Chain	Residue
A	TPP1
A	ASP155
A	ASN185
A	LEU187
A	HOH627

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT A 622

Chain	Residue
A	SER345
A	HIS416
A	ARG474
A	HOH895

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 623

Chain	Residue
A	TYR564
A	ALA588
A	ASN590
A	HOH643
A	HOH726

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 624

Chain	Residue
A	GLN189
A	SER256
A	TRP257
A	HIS258
A	HOH630
A	HOH745
B	ASN344

site_id	AC6
Number of Residues	25
Details	BINDING SITE FOR RESIDUE TPP B 1

Chain	Residue
A	ASP341
A	ILE364
A	GLU366
A	PHE392
A	ARG395
A	GLN428
B	SER40
B	LYS75
B	HIS77
B	GLY123
B	SER124
B	LEU125
B	GLY154
B	ASP155
B	GLY156
B	GLU157
B	GLU160
B	ASN185
B	LEU187
B	GLY188
B	GLN189
B	LYS244
B	HIS258
B	CA621
B	HOH627

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 621

Chain	Residue
B	TPP1
B	ASP155
B	ASN185
B	LEU187
B	HOH627

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT B 622

Chain	Residue
B	PHE142
B	ASP333
B	ARG381

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT B 623

Chain	Residue
B	SER345
B	HIS416
B	ARG474
B	HOH727
B	HOH756

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 624

Chain	Residue
B	TYR564
B	ALA588
B	ASN590
B	HOH663
B	HOH888

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 625

Chain	Residue
B	PRO63
B	ASN68
B	ASP69
B	ARG70
B	PHE71
B	ARG379
B	HOH887

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 626

Chain	Residue
B	TRP257
B	HIS258
B	HOH703
B	HOH862
A	ASN344
B	GLN189
B	SER256

Functional Information from PROSITE/UniProt

site_id	PS00801
Number of Residues	21
Details	TRANSKETOLASE_1 Transketolase signature 1. RissIQattaagSGHPTscCS

Chain	Residue	Details
A	ARG23-SER43

site_id	PS00802
Number of Residues	17
Details	TRANSKETOLASE_2 Transketolase signature 2. GEDGPSQmALEdlAmfR

Chain	Residue	Details
A	GLY422-ARG438

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"31534226","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23965678","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20667822","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23965678","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31534226","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MOS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OOY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RJB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8WA8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23965678","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4KXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PDB","id":"3OOY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23965678","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31534226","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KXU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HA3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6RJB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23965678","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KXV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KXX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"journal article","publicationDate":"2024","firstPage":"355","lastPage":"365","volume":"14","journal":"ACS Catal.","title":"Multifaceted Role of the Substrate Phosphate Group in Transketolase Catalysis.","authors":["Liu Z.","Xiao C.","Lin S.","Tittmann K.","Dai S."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/acscatal.3c04543"}]}},{"source":"PDB","id":"8WAA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"23965678","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P40142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50137","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)