1P1I
Crystal structure of the NAD+-bound 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 | 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 | 26 |
Details | BINDING SITE FOR RESIDUE NAD A 650 |
Chain | Residue |
A | ILE71 |
A | ILE185 |
A | ARG198 |
A | THR244 |
A | ALA245 |
A | ASN246 |
A | THR247 |
A | GLY295 |
A | SER296 |
A | PRO297 |
A | ASP320 |
A | GLY72 |
A | LEU321 |
A | ASN354 |
A | ASN355 |
A | ASP356 |
A | ALA442 |
A | HOH657 |
A | HOH700 |
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 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 | ASP438 |
B | LYS489 |
B | HOH686 |
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 |