3D5E
Crystal structure of human plasma platelet activating factor acetylhydrolase covalently inhibited by paraoxon
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003847 | molecular_function | 1-alkyl-2-acetylglycerophosphocholine esterase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005543 | molecular_function | phospholipid binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0009395 | biological_process | phospholipid catabolic process |
| A | 0016486 | biological_process | peptide hormone processing |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0034362 | cellular_component | low-density lipoprotein particle |
| A | 0034364 | cellular_component | high-density lipoprotein particle |
| A | 0034374 | biological_process | low-density lipoprotein particle remodeling |
| A | 0034440 | biological_process | lipid oxidation |
| A | 0034441 | biological_process | plasma lipoprotein particle oxidation |
| A | 0034638 | biological_process | phosphatidylcholine catabolic process |
| A | 0046469 | biological_process | platelet activating factor metabolic process |
| A | 0047499 | molecular_function | calcium-independent phospholipase A2 activity |
| A | 0050729 | biological_process | positive regulation of inflammatory response |
| A | 0062234 | biological_process | platelet activating factor catabolic process |
| A | 0090026 | biological_process | positive regulation of monocyte chemotaxis |
| B | 0003847 | molecular_function | 1-alkyl-2-acetylglycerophosphocholine esterase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0009395 | biological_process | phospholipid catabolic process |
| B | 0016486 | biological_process | peptide hormone processing |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0034362 | cellular_component | low-density lipoprotein particle |
| B | 0034364 | cellular_component | high-density lipoprotein particle |
| B | 0034374 | biological_process | low-density lipoprotein particle remodeling |
| B | 0034440 | biological_process | lipid oxidation |
| B | 0034441 | biological_process | plasma lipoprotein particle oxidation |
| B | 0034638 | biological_process | phosphatidylcholine catabolic process |
| B | 0046469 | biological_process | platelet activating factor metabolic process |
| B | 0047499 | molecular_function | calcium-independent phospholipase A2 activity |
| B | 0050729 | biological_process | positive regulation of inflammatory response |
| B | 0062234 | biological_process | platelet activating factor catabolic process |
| B | 0090026 | biological_process | positive regulation of monocyte chemotaxis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DEP A 473 |
| Chain | Residue |
| A | GLY152 |
| A | LEU153 |
| A | SER273 |
| A | PHE274 |
| A | TRP298 |
| A | PHE322 |
| A | HIS351 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE FMT A 2 |
| Chain | Residue |
| A | ASN135 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 3 |
| Chain | Residue |
| A | LYS252 |
| A | ASP254 |
| A | GLN257 |
| A | ASN135 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 4 |
| Chain | Residue |
| A | GLU256 |
| A | GLN257 |
| A | LYS259 |
| A | HOH509 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT A 5 |
| Chain | Residue |
| A | PHE300 |
| A | ALA326 |
| A | LYS330 |
| A | HOH528 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 11 |
| Chain | Residue |
| A | THR54 |
| A | MET128 |
| A | THR129 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT A 12 |
| Chain | Residue |
| A | VAL379 |
| A | ASP382 |
| A | LYS386 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 16 |
| Chain | Residue |
| A | ARG182 |
| A | THR208 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DEP B 473 |
| Chain | Residue |
| B | GLY152 |
| B | LEU153 |
| B | SER273 |
| B | PHE274 |
| B | TRP298 |
| B | HIS351 |
| B | GLN352 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT B 1 |
| Chain | Residue |
| B | TRP298 |
| B | TYR324 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 6 |
| Chain | Residue |
| B | TYR335 |
| B | LYS342 |
| B | MET343 |
| B | HOH518 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 7 |
| Chain | Residue |
| B | ARG182 |
| B | TRP203 |
| B | LEU204 |
| B | TYR205 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT B 8 |
| Chain | Residue |
| B | SER230 |
| B | GLN231 |
| B | SER234 |
| B | ARG288 |
| B | HOH554 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 9 |
| Chain | Residue |
| A | ILE422 |
| A | ASN423 |
| B | GLU320 |
| B | GLN323 |
| B | ASN421 |
| B | ILE422 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 10 |
| Chain | Residue |
| B | PRO57 |
| B | ARG58 |
| B | ALA162 |
| B | ASP166 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 13 |
| Chain | Residue |
| A | PRO311 |
| B | LYS143 |
| B | ILE262 |
| B | ARG264 |
| B | HOH605 |
| B | HOH606 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 14 |
| Chain | Residue |
| B | SER234 |
| B | ARG288 |
| B | HOH590 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 15 |
| Chain | Residue |
| B | GLN393 |
| B | LYS394 |
| B | ASP403 |
| B | HOH498 |
Functional Information from PROSITE/UniProt
| site_id | PS00120 |
| Number of Residues | 10 |
| Details | LIPASE_SER Lipases, serine active site. IAVIGHSFGG |
| Chain | Residue | Details |
| A | ILE267-GLY276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:18784071 |
| Chain | Residue | Details |
| A | SER273 | |
| B | SER273 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:18784071 |
| Chain | Residue | Details |
| A | ASP296 | |
| A | HIS351 | |
| B | ASP296 | |
| B | HIS351 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN423 | |
| B | ASN423 |
