Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MOS

The structure of human Transketolase

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	25
Details	BINDING SITE FOR RESIDUE TPP A 700

Chain	Residue
A	CA1
A	GLY156
A	GLU157
A	GLU160
A	ASN185
A	LEU187
A	GLY188
A	GLN189
A	LYS244
A	HIS258
A	ASP341
A	SER40
A	ILE364
A	GLU366
A	PHE392
A	ARG395
A	GLN428
A	HOH629
A	LYS75
A	HIS77
A	GLY123
A	SER124
A	LEU125
A	GLY154
A	ASP155

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 1

Chain	Residue
A	ASP155
A	ASN185
A	LEU187
A	HOH629
A	TPP700

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 619

Chain	Residue
A	GLN127
A	SER371
A	VAL374
A	GLN399
A	MET402
A	ALA403
A	HOH933

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 2

Chain	Residue
A	PRO441
A	LYS538
A	TYR563
A	TYR564
A	GLU565
A	VAL589
A	ASN590
A	HOH792
A	HOH981

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 620

Chain	Residue
A	LEU158
A	SER159
A	TRP164
A	TRP164
A	GLU165
A	ALA168
A	PHE209
A	EDO624

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 621

Chain	Residue
A	GLN189
A	SER256
A	TRP257
A	HIS258
A	ASN344
A	HOH688
A	HOH924

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 622

Chain	Residue
A	TYR564
A	ALA588
A	ASN590
A	HOH678
A	HOH761
A	HOH766
A	HOH968

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 623

Chain	Residue
A	ARG21
A	ALA84
A	GLU88
A	GLU94
A	LEU97

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 624

Chain	Residue
A	LEU158
A	TRP164
A	ARG205
A	PHE209
A	EDO620
A	HOH644

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 625

Chain	Residue
A	PRO63
A	ASN68
A	ASP69
A	ARG70
A	PHE71
A	ARG379
A	HOH835

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 626

Chain	Residue
A	ALA14
A	ASN590
A	ARG591
A	HOH1029

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 627

Chain	Residue
A	PHE71
A	VAL72
A	LEU73
A	LEU82
A	PHE117
A	HOH666
A	HOH670
A	HOH717

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 628

Chain	Residue
A	ALA461
A	THR464
A	CYS468
A	HOH657
A	HOH691
A	ASN411

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	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER3
A	SER104

site_id	SWS_FT_FI6
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_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P40142

Chain	Residue	Details
A	LYS232
A	LYS538

site_id	SWS_FT_FI8
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_FI9
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_FI10
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_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P50137

Chain	Residue	Details
A	SER345

site_id	SWS_FT_FI12
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)