6OHR
Structure of compound 5 bound human Phospholipase D1 catalytic domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004630 | molecular_function | phospholipase D activity |
| A | 0006654 | biological_process | phosphatidic acid biosynthetic process |
| A | 0035556 | biological_process | intracellular signal transduction |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004630 | molecular_function | phospholipase D activity |
| B | 0006654 | biological_process | phosphatidic acid biosynthetic process |
| B | 0035556 | biological_process | intracellular signal transduction |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004630 | molecular_function | phospholipase D activity |
| C | 0006654 | biological_process | phosphatidic acid biosynthetic process |
| C | 0035556 | biological_process | intracellular signal transduction |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004630 | molecular_function | phospholipase D activity |
| D | 0006654 | biological_process | phosphatidic acid biosynthetic process |
| D | 0035556 | biological_process | intracellular signal transduction |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004630 | molecular_function | phospholipase D activity |
| E | 0006654 | biological_process | phosphatidic acid biosynthetic process |
| E | 0035556 | biological_process | intracellular signal transduction |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004630 | molecular_function | phospholipase D activity |
| F | 0006654 | biological_process | phosphatidic acid biosynthetic process |
| F | 0035556 | biological_process | intracellular signal transduction |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue MKG A 1101 |
| Chain | Residue |
| A | TRP381 |
| A | PHE789 |
| A | ASN875 |
| A | ASN877 |
| A | ARG879 |
| D | LYS1026 |
| D | GLU1027 |
| D | ILE1029 |
| A | GLY428 |
| A | HIS464 |
| A | ARG486 |
| A | PHE614 |
| A | TRP640 |
| A | GLN744 |
| A | PHE745 |
| A | GLY788 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue MKG C 1101 |
| Chain | Residue |
| B | LYS1026 |
| B | GLU1027 |
| B | ILE1029 |
| C | TRP381 |
| C | TRP382 |
| C | GLY428 |
| C | HIS464 |
| C | ARG486 |
| C | TRP640 |
| C | GLN744 |
| C | PHE745 |
| C | GLY788 |
| C | PHE789 |
| C | ASN875 |
| C | ASN877 |
| C | ARG879 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue MKG D 1101 |
| Chain | Residue |
| A | LYS1026 |
| A | GLU1027 |
| A | ILE1029 |
| D | TRP381 |
| D | TRP382 |
| D | GLY428 |
| D | HIS464 |
| D | ARG486 |
| D | TRP640 |
| D | GLN744 |
| D | PHE745 |
| D | GLY788 |
| D | PHE789 |
| D | ASN875 |
| D | ASN877 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue MKG E 1101 |
| Chain | Residue |
| E | TRP381 |
| E | TRP382 |
| E | GLY428 |
| E | HIS464 |
| E | ARG486 |
| E | PHE614 |
| E | TRP640 |
| E | GLN744 |
| E | PHE745 |
| E | PHE789 |
| E | ASN875 |
| E | ASN877 |
| F | LYS1026 |
| F | GLU1027 |
| F | ILE1029 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue MKG F 1101 |
| Chain | Residue |
| E | LYS1026 |
| E | GLU1027 |
| F | TRP381 |
| F | TRP382 |
| F | GLY428 |
| F | ILE429 |
| F | HIS464 |
| F | ARG486 |
| F | TRP640 |
| F | GLN744 |
| F | GLY788 |
| F | PHE789 |
| F | ASN875 |
| F | ARG879 |
| F | VAL1034 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P70496 |
| Chain | Residue | Details |
| A | SER499 | |
| B | SER579 | |
| C | SER499 | |
| D | SER579 | |
| E | SER579 | |
| F | SER579 |
