1JKF
Holo 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 | 25 |
Details | BINDING SITE FOR RESIDUE NAD B 610 |
Chain | Residue |
B | GLY72 |
B | GLN195 |
B | ASP196 |
B | GLU197 |
B | THR244 |
B | ALA245 |
B | ASN246 |
B | THR247 |
B | SER296 |
B | PRO297 |
B | ASP320 |
B | GLY74 |
B | LEU321 |
B | LYS322 |
B | SER323 |
B | ALA442 |
B | HOH702 |
B | HOH834 |
B | GLY75 |
B | ASN76 |
B | ASN77 |
B | ASP148 |
B | ILE149 |
B | SER184 |
B | ASN194 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD A 600 |
Chain | Residue |
A | ILE71 |
A | GLY72 |
A | GLY74 |
A | GLY75 |
A | ASN76 |
A | ASN77 |
A | ASP148 |
A | ILE149 |
A | SER184 |
A | ASN194 |
A | ASP196 |
A | GLU197 |
A | TRP243 |
A | THR244 |
A | ALA245 |
A | ASN246 |
A | THR247 |
A | SER296 |
A | LEU321 |
A | LYS322 |
A | SER323 |
A | GLY409 |
A | ASP438 |
A | HOH613 |
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 | GLN52 | |
B | GLN52 |
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 | ASP53 | |
B | ASP53 |
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 | TYR54 | |
B | ARG225 | |
A | VAL55 | |
A | VAL126 | |
A | ILE223 | |
A | ARG225 | |
B | TYR54 | |
B | VAL55 | |
B | VAL126 | |
B | ILE223 |
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 | GLN162 | |
B | GLN162 |
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 | VAL163 | |
A | MET176 | |
B | VAL163 | |
B | MET176 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11779862, ECO:0007744|PDB:1JKF |
Chain | Residue | Details |
A | LYS173 | |
A | ALA174 | |
A | ASN299 | |
A | LEU387 | |
B | LYS173 | |
B | ALA174 | |
B | ASN299 | |
B | LEU387 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12836703, ECO:0007744|PDB:1LA2 |
Chain | Residue | Details |
A | ARG222 | |
B | ARG222 |
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 | ARG224 | |
B | ARG224 |
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 | GLU273 | |
B | GLU273 |
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 | GLU274 | |
A | ALA333 | |
B | GLU274 | |
B | ALA333 |
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 | GLN298 | |
B | GLN298 |
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 | PHE301 | |
B | PHE301 |
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 | LEU332 | |
B | LEU332 |
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 | GLN334 | |
B | GLN334 |
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 | ALA347 | |
B | ALA347 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11779862, ECO:0007744|PDB:1JKI |
Chain | Residue | Details |
A | TYR388 | |
B | TYR388 |
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 | ASP416 | |
B | ASP416 |
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 | GLU417 | |
B | GLU417 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:23902760 |
Chain | Residue | Details |
A | LEU26 | |
B | LEU26 |
site_id | SWS_FT_FI20 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:23902760 |
Chain | Residue | Details |
A | TYR155 | |
A | GLN162 | |
A | GLU274 | |
B | TYR155 | |
B | GLN162 | |
B | GLU274 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | ILE346 | |
B | ILE346 |
site_id | SWS_FT_FI22 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000305|PubMed:23902760 |
Chain | Residue | Details |
A | LEU352 | |
B | LEU352 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 331 |
Chain | Residue | Details |
A | GLN298 | electrostatic stabiliser, hydrogen bond acceptor |
A | ALA347 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ASP390 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | VAL467 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 331 |
Chain | Residue | Details |
B | GLN298 | electrostatic stabiliser, hydrogen bond acceptor |
B | ALA347 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ASP390 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | VAL467 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |