eF-site ID 1jkf-A
PDB Code 1jkf
Chain A

click to enlarge
Title Holo 1L-myo-inositol-1-phosphate Synthase
Classification ISOMERASE
Compound myo-inositol-1-phosphate synthase
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (INO1_YEAST)
Sequence A:  SVKVVTDKCTYKDNELLTKYSYENAVVTKTASGRFDVTPT
VQDYVFKLDLKKPEKLGIMLIGLGGNNGSTLVASVLANKH
NVEFQTKEGVKQPNYFGSMTQCSTLKLGIDAEGNDVYAPF
NSLLPMVSPNDFVVSGWDINNADLYEAMQRSQVLEYDLQQ
RLKAKMSLVKPLPSIYYPDFIAANQDERANNCINLDEKGN
VTTRGKWTHLQRIRRDIQNFKEENALDKVIVLWTANTERY
VEVSPGVNDTMENLLQSIKNDHEEIAPSTIFAAASILEGV
PYINGSPQNTFVPGLVQLAEHEGTFIAGDDLKSGQTKLKS
VLAQFLVDAGIKPVSIASYNHGDSKVAMDEYYSELMLGGH
NRISIHNVCEDSLLATPLIIDLLVMTEFCTRVSYKKVDPV
KEDAGKFENFYPVLTFLSYWLKAPLTRPGFHPVNGLNKQR
TALENFLRLLIGLPSQNELRFEERLL
Description (1)  myo-inositol-1-phosphate synthase (E.C.5.5.1.4)


Functional site
1) chain A
residue 71
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
2) chain A
residue 72
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
3) chain A
residue 74
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
4) chain A
residue 75
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
5) chain A
residue 76
type
sequence N
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
6) chain A
residue 77
type
sequence N
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
7) chain A
residue 148
type
sequence D
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
8) chain A
residue 149
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
9) chain A
residue 184
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
10) chain A
residue 194
type
sequence N
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
11) chain A
residue 196
type
sequence D
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
12) chain A
residue 197
type
sequence E
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
13) chain A
residue 243
type
sequence W
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
14) chain A
residue 244
type
sequence T
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
15) chain A
residue 245
type
sequence A
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
16) chain A
residue 246
type
sequence N
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
17) chain A
residue 247
type
sequence T
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
18) chain A
residue 296
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
19) chain A
residue 321
type
sequence L
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
20) chain A
residue 322
type
sequence K
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
21) chain A
residue 323
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
22) chain A
residue 409
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
23) chain A
residue 438
type
sequence D
description BINDING SITE FOR RESIDUE NAD A 600
source : AC2
24) chain A
residue 298
type catalytic
sequence Q
description 331
source MCSA : MCSA1
25) chain A
residue 347
type catalytic
sequence A
description 331
source MCSA : MCSA1
26) chain A
residue 467
type catalytic
sequence V
description 331
source MCSA : MCSA1
27) chain A
residue 274
type BINDING
sequence E
description 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
source Swiss-Prot : SWS_FT_FI10
28) chain A
residue 333
type BINDING
sequence A
description 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
source Swiss-Prot : SWS_FT_FI10
29) chain A
residue 298
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:11779862, ECO:0000269|PubMed:12832758, ECO:0007744|PDB:1JKF, ECO:0007744|PDB:1P1H
source Swiss-Prot : SWS_FT_FI11
30) chain A
residue 301
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:11779862, ECO:0000269|PubMed:12832758, ECO:0007744|PDB:1JKF, ECO:0007744|PDB:1P1J
source Swiss-Prot : SWS_FT_FI12
31) chain A
residue 332
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:12832758, ECO:0000269|PubMed:12836703, ECO:0007744|PDB:1LA2, ECO:0007744|PDB:1P1H
source Swiss-Prot : SWS_FT_FI13
32) chain A
residue 334
type BINDING
sequence Q
description 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
source Swiss-Prot : SWS_FT_FI14
33) chain A
residue 347
type BINDING
sequence A
description 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
source Swiss-Prot : SWS_FT_FI15
34) chain A
residue 416
type BINDING
sequence D
description 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
source Swiss-Prot : SWS_FT_FI17
35) chain A
residue 417
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11779862, ECO:0000269|PubMed:12832758, ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1P1H, ECO:0007744|PDB:1P1K
source Swiss-Prot : SWS_FT_FI18
36) chain A
residue 26
type MOD_RES
sequence L
description Phosphothreonine => ECO:0000269|PubMed:23902760
source Swiss-Prot : SWS_FT_FI19
37) chain A
residue 53
type BINDING
sequence D
description 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
source Swiss-Prot : SWS_FT_FI2
38) chain A
residue 155
type MOD_RES
sequence Y
description Phosphoserine => ECO:0000269|PubMed:23902760
source Swiss-Prot : SWS_FT_FI20
39) chain A
residue 162
type MOD_RES
sequence Q
description Phosphoserine => ECO:0000269|PubMed:23902760
source Swiss-Prot : SWS_FT_FI20
40) chain A
residue 274
type MOD_RES
sequence E
description Phosphoserine => ECO:0000269|PubMed:23902760
source Swiss-Prot : SWS_FT_FI20
41) chain A
residue 346
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI21
42) chain A
residue 54
type BINDING
sequence Y
description 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
source Swiss-Prot : SWS_FT_FI3
43) chain A
residue 55
type BINDING
sequence V
description 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
source Swiss-Prot : SWS_FT_FI3
44) chain A
residue 126
type BINDING
sequence V
description 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
source Swiss-Prot : SWS_FT_FI3
45) chain A
residue 223
type BINDING
sequence I
description 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
source Swiss-Prot : SWS_FT_FI3
46) chain A
residue 225
type BINDING
sequence R
description 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
source Swiss-Prot : SWS_FT_FI3
47) chain A
residue 162
type BINDING
sequence Q
description 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
source Swiss-Prot : SWS_FT_FI4
48) chain A
residue 163
type BINDING
sequence V
description 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
source Swiss-Prot : SWS_FT_FI5
49) chain A
residue 176
type BINDING
sequence M
description 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
source Swiss-Prot : SWS_FT_FI5
50) chain A
residue 173
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:11779862, ECO:0007744|PDB:1JKF
source Swiss-Prot : SWS_FT_FI6
51) chain A
residue 174
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:11779862, ECO:0007744|PDB:1JKF
source Swiss-Prot : SWS_FT_FI6
52) chain A
residue 299
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:11779862, ECO:0007744|PDB:1JKF
source Swiss-Prot : SWS_FT_FI6
53) chain A
residue 222
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:12836703, ECO:0007744|PDB:1LA2
source Swiss-Prot : SWS_FT_FI7
54) chain A
residue 224
type BINDING
sequence R
description 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
source Swiss-Prot : SWS_FT_FI8
55) chain A
residue 273
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:11779862, ECO:0000269|PubMed:12832758, ECO:0007744|PDB:1JKI, ECO:0007744|PDB:1P1H
source Swiss-Prot : SWS_FT_FI9
56) chain A
residue 52
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:11779862, ECO:0000269|PubMed:12836703, ECO:0007744|PDB:1JKF, ECO:0007744|PDB:1LA2
source Swiss-Prot : SWS_FT_FI1

Display surface

Download
Links