Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KXU

Human transketolase in covalent complex with donor ketose D-fructose-6-phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
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	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0005789	cellular_component	endoplasmic reticulum membrane
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	0016740	molecular_function	transferase activity
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0031982	cellular_component	vesicle
A	0040008	biological_process	regulation of growth
A	0042803	molecular_function	protein homodimerization activity
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	1901159	biological_process	xylulose 5-phosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 1001

Chain	Residue
A	SER35
A	GLY36
A	HIS37
A	GLY259
A	ASP424
A	ARG474
A	S6P1014
A	HOH7105
A	HOH7207

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1002

Chain	Residue
A	PHE71
A	VAL72
A	LEU73
A	LEU82
A	PHE117
A	HOH7010
A	HOH7043
A	HOH7078

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1003

Chain	Residue
A	TYR564
A	ALA588
A	ASN590
A	HOH7037
A	HOH7057
A	HOH7102
A	HOH7357

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO A 1004

Chain	Residue
A	ARG21
A	SER25
A	ALA84
A	GLU88
A	GLU94
A	LEU97
A	LYS283
A	HOH7239
A	HOH7485
A	HOH7721

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1005

Chain	Residue
A	PRO63
A	ASN68
A	ASP69
A	ARG70
A	PHE71
A	ARG379
A	HOH7378

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 1006

Chain	Residue
A	ASP155
A	ASN185
A	LEU187
A	TPP1015
A	HOH7009

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 1007

Chain	Residue
A	ALA33
A	ARG101
A	GLU423
A	LYS597
A	HOH7222

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1008

Chain	Residue
A	LEU92
A	ASP106
A	LEU107
A	GLN115
A	HOH7095
A	HOH7131
A	HOH7133

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1009

Chain	Residue
A	ASN411
A	ALA461
A	THR464
A	CYS468
A	HOH7084
A	HOH7101

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1010

Chain	Residue
A	LYS11
A	PHE53
A	HIS54
A	ARG57
A	THR287
A	HOH7130
A	HOH7223

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1011

Chain	Residue
A	GLN10
A	LYS11
A	ILE284
A	ASN590
A	ARG591
A	HOH7347
A	HOH7803

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1012

Chain	Residue
A	TYR137
A	TYR141
A	TYR173
A	HOH7193
A	HOH7261
A	HOH7766

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE EDO A 1013

Chain	Residue
A	ASP155
A	GLY156
A	LEU158
A	SER159
A	TRP164
A	PRO194
A	LEU195
A	TYR202
A	ARG205
A	HOH7176
A	HOH7746
A	HOH7799

site_id	BC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE S6P A 1014

Chain	Residue
A	GLY123
A	GLN189
A	HIS258
A	ARG318
A	SER345
A	PHE389
A	HIS416
A	ASP424
A	GLN428
A	ARG474
A	EDO1001
A	TPP1015
A	HOH7056
A	HOH7157
A	HOH7235
A	HOH7269
A	HOH7723
A	HOH7783
A	HOH7784
A	HOH7785
A	HIS37
A	HIS77
A	HIS110

site_id	BC6
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TPP A 1015

Chain	Residue
A	SER40
A	LYS75
A	HIS77
A	GLY123
A	SER124
A	LEU125
A	GLY154
A	ASP155
A	GLY156
A	GLU157
A	GLU160
A	ASN185
A	LEU187
A	GLY188
A	GLN189
A	LYS244
A	HIS258
A	ASP341
A	ILE364
A	GLU366
A	PHE392
A	ARG395
A	GLN428
A	MG1006
A	S6P1014
A	HOH7009

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	1
Details	ACT_SITE: Proton donor => ECO:0000250

Chain	Residue	Details
A	GLU366

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	HIS37
A	ARG318
A	SER345
A	HIS416
A	ASP424
A	ARG474

site_id	SWS_FT_FI3
Number of Residues	11
Details	BINDING:

Chain	Residue	Details
A	SER40
A	PHE392
A	GLN428
A	HIS77
A	GLY123
A	ASP155
A	GLY156
A	ASN185
A	LEU187
A	LYS244
A	HIS258

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000250

Chain	Residue	Details
A	HIS37
A	HIS258

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	MET1

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER3
A	SER104

site_id	SWS_FT_FI7
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS6
A	LYS11
A	LYS144
A	LYS204
A	LYS241
A	LYS260
A	LYS603

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P40142

Chain	Residue	Details
A	LYS232
A	LYS538

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
A	TYR275

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	THR287

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER295

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P50137

Chain	Residue	Details
A	SER345

site_id	SWS_FT_FI13
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
A	LYS352

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