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	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	0006796	biological_process	phosphate-containing compound metabolic process
A	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
A	0016604	cellular_component	nuclear body
A	0016740	molecular_function	transferase activity
A	0016744	molecular_function	transketolase or transaldolase activity
A	0019637	biological_process	organophosphate metabolic process
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	1901135	biological_process	carbohydrate derivative metabolic process
A	1901159	biological_process	xylulose 5-phosphate biosynthetic process
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
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	0005737	cellular_component	cytoplasm
B	0005777	cellular_component	peroxisome
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0006098	biological_process	pentose-phosphate shunt
B	0006796	biological_process	phosphate-containing compound metabolic process
B	0009052	biological_process	pentose-phosphate shunt, non-oxidative branch
B	0016604	cellular_component	nuclear body
B	0016740	molecular_function	transferase activity
B	0016744	molecular_function	transketolase or transaldolase activity
B	0019637	biological_process	organophosphate metabolic process
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0031982	cellular_component	vesicle
B	0040008	biological_process	regulation of growth
B	0042803	molecular_function	protein homodimerization activity
B	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome
B	1901135	biological_process	carbohydrate derivative metabolic process
B	1901159	biological_process	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	ACT_SITE: Proton donor => ECO:0000250

Chain	Residue	Details
A	GLU366
B	GLU366

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000250

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

---

site_id	SWS_FT_FI3
Number of Residues	22
Details	BINDING:

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

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Important for catalytic activity => ECO:0000250

Chain	Residue	Details
A	HIS37
A	HIS258
B	HIS37
B	HIS258

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	MET1
B	MET1

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER3
A	SER104
B	SER3
B	SER104

---

site_id	SWS_FT_FI7
Number of Residues	14
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

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

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P40142

Chain	Residue	Details
A	LYS232
A	LYS538
B	LYS232
B	LYS538

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	TYR275
B	TYR275

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	THR287
B	THR287

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER295
B	SER295

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P50137

Chain	Residue	Details
A	SER345
B	SER345

---

site_id	SWS_FT_FI13
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733

Chain	Residue	Details
A	LYS352
B	LYS352

---