8WA8

Human transketolase in complex with phosphite

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 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

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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

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