Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JKF

Holo 1L-myo-inositol-1-phosphate Synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004512	molecular_function	inositol-3-phosphate synthase activity
A	0005737	cellular_component	cytoplasm
A	0006021	biological_process	inositol biosynthetic process
A	0006629	biological_process	lipid metabolic process
A	0008654	biological_process	phospholipid biosynthetic process
A	0016853	molecular_function	isomerase activity
B	0004512	molecular_function	inositol-3-phosphate synthase activity
B	0005737	cellular_component	cytoplasm
B	0006021	biological_process	inositol biosynthetic process
B	0006629	biological_process	lipid metabolic process
B	0008654	biological_process	phospholipid biosynthetic process
B	0016853	molecular_function	isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD B 610

Chain	Residue
B	GLY72
B	GLN195
B	ASP196
B	GLU197
B	THR244
B	ALA245
B	ASN246
B	THR247
B	SER296
B	PRO297
B	ASP320
B	GLY74
B	LEU321
B	LYS322
B	SER323
B	ALA442
B	HOH702
B	HOH834
B	GLY75
B	ASN76
B	ASN77
B	ASP148
B	ILE149
B	SER184
B	ASN194

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD A 600

Chain	Residue
A	ILE71
A	GLY72
A	GLY74
A	GLY75
A	ASN76
A	ASN77
A	ASP148
A	ILE149
A	SER184
A	ASN194
A	ASP196
A	GLU197
A	TRP243
A	THR244
A	ALA245
A	ASN246
A	THR247
A	SER296
A	LEU321
A	LYS322
A	SER323
A	GLY409
A	ASP438
A	HOH613

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12836703, ECO:0007744\|PDB:1JKF, ECO:0007744\|PDB:1LA2

Chain	Residue	Details
A	GLN52
B	GLN52

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:12836703, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1JKF, ECO:0007744\|PDB:1LA2, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1I, ECO:0007744\|PDB:1P1J, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	ASP53
B	ASP53

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:12836703, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1JKF, ECO:0007744\|PDB:1JKI, ECO:0007744\|PDB:1LA2, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1I, ECO:0007744\|PDB:1P1J, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	TYR54
B	ARG225
A	VAL55
A	VAL126
A	ILE223
A	ARG225
B	TYR54
B	VAL55
B	VAL126
B	ILE223

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1JKF, ECO:0007744\|PDB:1JKI, ECO:0007744\|PDB:1LA2, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1I, ECO:0007744\|PDB:1P1J, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	GLN162
B	GLN162

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:12836703, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1JKI, ECO:0007744\|PDB:1LA2, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1I, ECO:0007744\|PDB:1P1J, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	VAL163
A	MET176
B	VAL163
B	MET176

site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0007744\|PDB:1JKF

Chain	Residue	Details
A	LYS173
A	ALA174
A	ASN299
A	LEU387
B	LYS173
B	ALA174
B	ASN299
B	LEU387

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:12836703, ECO:0007744\|PDB:1LA2

Chain	Residue	Details
A	ARG222
B	ARG222

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1JKF, ECO:0007744\|PDB:1JKI, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1I, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	ARG224
B	ARG224

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0007744\|PDB:1JKI, ECO:0007744\|PDB:1P1H

Chain	Residue	Details
A	GLU273
B	GLU273

site_id	SWS_FT_FI10
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:12836703, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1JKI, ECO:0007744\|PDB:1LA2, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1I, ECO:0007744\|PDB:1P1J, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	GLU274
A	ALA333
B	GLU274
B	ALA333

site_id	SWS_FT_FI11
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0007744\|PDB:1JKF, ECO:0007744\|PDB:1P1H

Chain	Residue	Details
A	GLN298
B	GLN298

site_id	SWS_FT_FI12
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0007744\|PDB:1JKF, ECO:0007744\|PDB:1P1J

Chain	Residue	Details
A	PHE301
B	PHE301

site_id	SWS_FT_FI13
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:12836703, ECO:0007744\|PDB:1LA2, ECO:0007744\|PDB:1P1H

Chain	Residue	Details
A	LEU332
B	LEU332

site_id	SWS_FT_FI14
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:12836703, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1JKI, ECO:0007744\|PDB:1LA2, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1J, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	GLN334
B	GLN334

site_id	SWS_FT_FI15
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1J, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	ALA347
B	ALA347

site_id	SWS_FT_FI16
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0007744\|PDB:1JKI

Chain	Residue	Details
A	TYR388
B	TYR388

site_id	SWS_FT_FI17
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:12832758, ECO:0000269\|PubMed:12836703, ECO:0000269\|PubMed:14684747, ECO:0007744\|PDB:1LA2, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1J, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	ASP416
B	ASP416

site_id	SWS_FT_FI18
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0000269\|PubMed:12832758, ECO:0007744\|PDB:1JKI, ECO:0007744\|PDB:1P1H, ECO:0007744\|PDB:1P1K

Chain	Residue	Details
A	GLU417
B	GLU417

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:23902760

Chain	Residue	Details
A	LEU26
B	LEU26

site_id	SWS_FT_FI20
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:23902760

Chain	Residue	Details
A	TYR155
A	GLN162
A	GLU274
B	TYR155
B	GLN162
B	GLU274

site_id	SWS_FT_FI21
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19779198

Chain	Residue	Details
A	ILE346
B	ILE346

site_id	SWS_FT_FI22
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000305\|PubMed:23902760

Chain	Residue	Details
A	LEU352
B	LEU352

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 331

Chain	Residue	Details
A	GLN298	electrostatic stabiliser, hydrogen bond acceptor
A	ALA347	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP390	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	VAL467	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 331

Chain	Residue	Details
B	GLN298	electrostatic stabiliser, hydrogen bond acceptor
B	ALA347	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	ASP390	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	VAL467	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)