Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KXV

Human transketolase in covalent complex with donor ketose D-xylulose-5-phosphate, crystal 1

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	0005737	cellular_component	cytoplasm
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	0016740	molecular_function	transferase activity
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	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	1901159	biological_process	D-xylulose 5-phosphate biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 1001

Chain	Residue
A	ASP155
A	ASN185
A	LEU187
A	TPP1011
A	HOH7001

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

Chain	Residue
A	PHE71
A	ARG379
A	HOH7185
A	HOH7887
A	PRO63
A	ASN68
A	ASP69
A	ARG70

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1003

Chain	Residue
A	PHE71
A	VAL72
A	LEU73
A	LEU82
A	PHE117
A	HOH7043
A	HOH7059
A	HOH7081

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1004

Chain	Residue
A	TYR564
A	ALA588
A	ASN590
A	HOH7035
A	HOH7051
A	HOH7134
A	HOH7250

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO A 1005

Chain	Residue
A	ARG21
A	SER25
A	ALA84
A	ALA87
A	GLU88
A	GLU94
A	LEU97
A	LYS283
A	HOH7317
A	HOH7643

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 1006

Chain	Residue
A	LEU92
A	ASP106
A	LEU107
A	GLN115
A	HOH7117
A	HOH7124
A	HOH7162

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1007

Chain	Residue
A	GLN10
A	LYS11
A	ASN590
A	ARG591
A	HOH7309
A	HOH7885

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EDO A 1008

Chain	Residue
A	ALA33
A	LEU100
A	ARG101
A	LYS102
A	GLU423
A	LYS597
A	HOH7104
A	HOH7916
A	HOH7935
A	HOH7948

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO A 1009

Chain	Residue
A	LEU158
A	TRP164
A	LEU195
A	ARG205
A	HOH7040
A	HOH7149
A	HOH7803
A	HOH7866

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 1010

Chain	Residue
A	TYR137
A	TYR141
A	TYR173
A	HOH7364
A	HOH7500
A	HOH7728

site_id	BC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE TPP A 1011

Chain	Residue
A	DX51012
A	HOH7001
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	CA1001

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE DX5 A 1012

Chain	Residue
A	HIS37
A	HIS77
A	HIS110
A	GLN189
A	HIS258
A	ARG318
A	SER345
A	PHE389
A	HIS416
A	ASP424
A	GLN428
A	ARG474
A	TPP1011
A	HOH7067
A	HOH7102
A	HOH7121
A	HOH7273
A	HOH7297
A	HOH7427
A	HOH7738
A	HOH7957

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	Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	7
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P40142","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
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_FI9
Number of Residues	1
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_FI10
Number of Residues	1
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_FI11
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P50137","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
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)