Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1JKI

myo-Inositol-1-phosphate Synthase Complexed with an Inhibitor, 2-deoxy-glucitol-6-phosphate

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	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	0008654	biological_process	phospholipid biosynthetic process
B	0016853	molecular_function	isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NH4 A 670

Chain	Residue
A	LEU352
A	ASN354
A	ASP438
A	DG6630
A	NAI650

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NH4 B 680

Chain	Residue
B	NAI660
B	LEU352
B	ASN354
B	ASP438
B	DG6640

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DG6 A 630

Chain	Residue
A	ASP320
A	SER323
A	GLN325
A	ASN350
A	ASP356
A	GLY357
A	LEU360
A	LYS369
A	ILE402
A	LYS412
A	LYS489
A	NAI650
A	NH4670

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DG6 B 640

Chain	Residue
B	SER323
B	GLN325
B	THR326
B	LEU352
B	ASN354
B	ASP356
B	GLY357
B	LEU360
B	LYS369
B	ILE402
B	LYS412
B	LYS489
B	NAI660
B	NH4680
B	HOH986
B	HOH995

site_id	AC5
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAI A 650

Chain	Residue
A	GLY72
A	GLY74
A	GLY75
A	ASN76
A	ASN77
A	ASP148
A	ILE149
A	SER184
A	ILE185
A	ARG198
A	THR244
A	ALA245
A	ASN246
A	THR247
A	GLY295
A	SER296
A	LEU321
A	ASN355
A	ASP356
A	LYS369
A	ASP410
A	ASP438
A	SER439
A	ALA442
A	DG6630
A	NH4670
A	HOH674
A	HOH777
A	HOH784
A	HOH892
A	HOH893

site_id	AC6
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAI B 660

Chain	Residue
B	GLY72
B	GLY75
B	ASN76
B	ASN77
B	ASP148
B	ILE149
B	SER184
B	ILE185
B	ARG198
B	THR244
B	ALA245
B	ASN246
B	THR247
B	GLY295
B	SER296
B	ASN355
B	ASP356
B	LYS369
B	ASP410
B	ASP438
B	SER439
B	DG6640
B	NH4680
B	HOH754
B	HOH755
B	HOH915
B	HOH969
B	HOH986

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)