Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8WAA

Human transketolase soaked with donor ketose D-xylulose

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 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	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	14
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","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)