Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1RM0

Crystal Structure of Myo-Inositol 1-Phosphate Synthase From Saccharomyces cerevisiae In Complex With NAD+ and 2-deoxy-D-glucitol 6-(E)-vinylhomophosphonate

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 MN A 630

Chain	Residue
A	ASN76
A	ASN77
A	ASP410
A	SER439
A	NAI650

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE D6P A 1520

Chain	Residue
A	LYS327
A	LEU352
A	ASP356
A	LEU360
A	LYS369
A	LYS373
A	ILE402
A	LYS412
A	ASP438
A	LYS489
A	NAI650
A	SER323
A	GLY324
A	GLN325
A	THR326

site_id	AC3
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAI A 650

Chain	Residue
A	ILE71
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	ASP320
A	LEU321
A	SER323
A	ASN355
A	ASP356
A	LYS369
A	ASP438
A	ALA442
A	MN630
A	HOH631
A	HOH662
A	HOH672
A	HOH687
A	HOH751
A	HOH770
A	HOH805
A	D6P1520

site_id	AC4
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAI B 660

Chain	Residue
B	ILE71
B	GLY72
B	GLY74
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	PRO297
B	ASP320
B	LEU321
B	SER323
B	ASN355
B	ASP356
B	LYS369
B	ASP438
B	ALA442
B	LYS489
B	HOH632
B	HOH664
B	HOH665
B	HOH686
B	HOH843
B	HOH908
B	HOH915

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	GLY74
B	GLY74

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	GLY75
B	GLY75

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	ASN76
B	THR247
A	ASN77
A	ASP148
A	ALA245
A	THR247
B	ASN76
B	ASN77
B	ASP148
B	ALA245

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	SER184
B	SER184

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	ILE185
A	ARG198
B	ILE185
B	ARG198

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

Chain	Residue	Details
A	GLN195
A	ASP196
A	LEU321
A	GLY409
B	GLN195
B	ASP196
B	LEU321
B	GLY409

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

Chain	Residue	Details
A	THR244
B	THR244

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	ASN246
B	ASN246

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	GLY295
B	GLY295

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	SER296
A	ASN355
B	SER296
B	ASN355

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	ASP320
B	ASP320

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	SER323
B	SER323

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	ASN354
B	ASN354

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	ASP356
B	ASP356

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	LYS369
B	LYS369

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

Chain	Residue	Details
A	ASP410
B	ASP410

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	ASP438
B	ASP438

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	SER439
B	SER439

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

Chain	Residue	Details
A	THR48
B	THR48

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

Chain	Residue	Details
A	SER177
A	SER184
A	SER296
B	SER177
B	SER184
B	SER296

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

Chain	Residue	Details
A	SER368
B	SER368

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

Chain	Residue	Details
A	SER374
B	SER374

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 331

Chain	Residue	Details
A	ASP320	electrostatic stabiliser, hydrogen bond acceptor
A	LYS369	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS412	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LYS489	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	4
Details	M-CSA 331

Chain	Residue	Details
B	ASP320	electrostatic stabiliser, hydrogen bond acceptor
B	LYS369	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LYS412	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LYS489	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)