Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1LA2

Structural analysis of Saccharomyces cerevisiae myo-inositol 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	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
C	0004512	molecular_function	inositol-3-phosphate synthase activity
C	0005737	cellular_component	cytoplasm
C	0006021	biological_process	inositol biosynthetic process
C	0008654	biological_process	phospholipid biosynthetic process
C	0016853	molecular_function	isomerase activity
D	0004512	molecular_function	inositol-3-phosphate synthase activity
D	0005737	cellular_component	cytoplasm
D	0006021	biological_process	inositol biosynthetic process
D	0008654	biological_process	phospholipid biosynthetic process
D	0016853	molecular_function	isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD A 900

Chain	Residue
A	ILE71
A	ILE185
A	ARG198
A	THR244
A	ALA245
A	ASN246
A	THR247
A	SER296
A	PRO297
A	LEU321
A	ASN355
A	GLY72
A	ASP356
A	ASP438
A	SER439
A	ALA442
A	HOH908
A	GLY74
A	GLY75
A	ASN76
A	ASN77
A	ASP148
A	ILE149
A	SER184

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD B 901

Chain	Residue
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	ASP320
B	ASN355
B	ASP356
B	ASP438
B	ALA442
B	HOH904
B	HOH947
B	HOH960

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD C 902

Chain	Residue
C	GLY72
C	GLY74
C	GLY75
C	ASN76
C	ASN77
C	ASP148
C	ILE149
C	SER184
C	ILE185
C	ARG198
C	THR244
C	ALA245
C	ASN246
C	THR247
C	GLY295
C	SER296
C	PRO297
C	LEU321
C	ASN355
C	ASP356
C	ASP438
C	ALA442
C	HOH903
C	HOH933
C	HOH995

site_id	AC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAD D 903

Chain	Residue
D	HOH920
D	HOH973
D	HOH1066
D	GLY72
D	GLY74
D	GLY75
D	ASN76
D	ASN77
D	ASP148
D	ILE149
D	SER184
D	ILE185
D	GLN195
D	ARG198
D	THR244
D	ALA245
D	ASN246
D	THR247
D	GLY295
D	SER296
D	PRO297
D	ASP320
D	LEU321
D	ASN354
D	ASN355
D	ASP356
D	ASP438
D	ALA442
D	HOH913
D	HOH914

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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
C	GLY74
D	GLY74

site_id	SWS_FT_FI2
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: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
C	GLY75
D	GLY75

site_id	SWS_FT_FI3
Number of Residues	20
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
C	ASN76
C	ASN77
C	ASP148
C	ALA245
C	THR247
D	ASN76
D	ASN77
D	ASP148
D	ALA245
A	ASN77
D	THR247
A	ASP148
A	ALA245
A	THR247
B	ASN76
B	ASN77
B	ASP148
B	ALA245

site_id	SWS_FT_FI4
Number of Residues	4
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
C	SER184
D	SER184

site_id	SWS_FT_FI5
Number of Residues	8
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
C	ILE185
C	ARG198
D	ILE185
D	ARG198

site_id	SWS_FT_FI6
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0007744\|PDB:1JKF

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

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:12836703, ECO:0007744\|PDB:1LA2

Chain	Residue	Details
A	THR244
B	THR244
C	THR244
D	THR244

site_id	SWS_FT_FI8
Number of Residues	4
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
C	ASN246
D	ASN246

site_id	SWS_FT_FI9
Number of Residues	4
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
C	GLY295
D	GLY295

site_id	SWS_FT_FI10
Number of Residues	8
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
C	SER296
C	ASN355
D	SER296
D	ASN355

site_id	SWS_FT_FI11
Number of Residues	4
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
C	ASP320
D	ASP320

site_id	SWS_FT_FI12
Number of Residues	4
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
C	SER323
D	SER323

site_id	SWS_FT_FI13
Number of Residues	4
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
C	ASN354
D	ASN354

site_id	SWS_FT_FI14
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:1P1J, ECO:0007744\|PDB:1P1K, ECO:0007744\|PDB:1RM0

Chain	Residue	Details
A	ASP356
B	ASP356
C	ASP356
D	ASP356

site_id	SWS_FT_FI15
Number of Residues	4
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
C	LYS369
D	LYS369

site_id	SWS_FT_FI16
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:11779862, ECO:0007744\|PDB:1JKI

Chain	Residue	Details
A	ASP410
B	ASP410
C	ASP410
D	ASP410

site_id	SWS_FT_FI17
Number of Residues	4
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
C	ASP438
D	ASP438

site_id	SWS_FT_FI18
Number of Residues	4
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
C	SER439
D	SER439

site_id	SWS_FT_FI19
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:23902760

Chain	Residue	Details
A	THR48
B	THR48
C	THR48
D	THR48

site_id	SWS_FT_FI20
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:23902760

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

site_id	SWS_FT_FI21
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19779198

Chain	Residue	Details
A	SER368
B	SER368
C	SER368
D	SER368

site_id	SWS_FT_FI22
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000305\|PubMed:23902760

Chain	Residue	Details
A	SER374
B	SER374
C	SER374
D	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

site_id	MCSA3
Number of Residues	4
Details	M-CSA 331

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

site_id	MCSA4
Number of Residues	4
Details	M-CSA 331

Chain	Residue	Details
D	ASP320	electrostatic stabiliser, hydrogen bond acceptor
D	LYS369	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	LYS412	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	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)