1P1H
Crystal structure of the 1L-myo-inositol/NAD+ complex
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 | 30 |
Details | BINDING SITE FOR RESIDUE NAD A 650 |
Chain | Residue |
A | ILE71 |
A | ILE185 |
A | ILE191 |
A | ARG198 |
A | THR244 |
A | ALA245 |
A | ASN246 |
A | THR247 |
A | GLY295 |
A | SER296 |
A | PRO297 |
A | GLY72 |
A | LEU321 |
A | ASN355 |
A | ASP356 |
A | ASP438 |
A | SER439 |
A | HOH652 |
A | HOH708 |
A | HOH824 |
A | HOH872 |
A | HOH1031 |
A | GLY74 |
A | HOH1061 |
A | GLY75 |
A | ASN76 |
A | ASN77 |
A | ASP148 |
A | ILE149 |
A | SER184 |
site_id | AC2 |
Number of Residues | 27 |
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 | ASN354 |
B | ASN355 |
B | ASP356 |
B | ASP438 |
B | ALA442 |
B | HOH691 |
B | HOH815 |
site_id | AC3 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE NAD C 670 |
Chain | Residue |
C | GLY72 |
C | GLY74 |
C | GLY75 |
C | ASN76 |
C | ASN77 |
C | ASP148 |
C | ILE149 |
C | SER184 |
C | ILE185 |
C | ILE191 |
C | ARG198 |
C | THR244 |
C | ALA245 |
C | ASN246 |
C | THR247 |
C | GLY295 |
C | SER296 |
C | LEU321 |
C | ASN355 |
C | ASP356 |
C | LYS369 |
C | ASP410 |
C | ASP438 |
C | SER439 |
C | HOH688 |
C | HOH736 |
C | HOH755 |
C | HOH778 |
C | HOH780 |
C | HOH782 |
C | HOH914 |
site_id | AC4 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAD D 680 |
Chain | Residue |
D | ARG198 |
D | THR244 |
D | ALA245 |
D | ASN246 |
D | THR247 |
D | GLY295 |
D | SER296 |
D | ASP320 |
D | ASN354 |
D | ASN355 |
D | ASP356 |
D | ASP438 |
D | SER439 |
D | HOH712 |
D | HOH778 |
D | HOH808 |
D | HOH820 |
D | HOH836 |
D | HOH997 |
D | ILE71 |
D | GLY72 |
D | GLY74 |
D | GLY75 |
D | ASN76 |
D | ASN77 |
D | ASP148 |
D | ILE149 |
D | SER184 |
D | ILE185 |
D | ILE191 |
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 |