5LP1
CRYSTAL STRUCTURE OF HUMAN LIPOPROTEIN-ASSOCIATED PHOSPHOLIPASE A2 IN COMPLEX WITH A [1.1.1]BICYCLOPENTANE-CONTAINING INHIBITOR AT 1.91A RESOLUTION.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003847 | molecular_function | 1-alkyl-2-acetylglycerophosphocholine esterase activity |
| A | 0004623 | molecular_function | phospholipase A2 activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005543 | molecular_function | phospholipid binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0009395 | biological_process | phospholipid catabolic process |
| A | 0016042 | biological_process | lipid 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 | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | PHE322 |
| A | HIS351 |
| A | HOH927 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 502 |
| Chain | Residue |
| A | ARG92 |
| A | LEU93 |
| A | PRO325 |
| A | ALA326 |
| A | HOH878 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue 71H A 503 |
| Chain | Residue |
| A | LEU111 |
| A | LEU121 |
| A | GLY152 |
| A | LEU153 |
| A | GLY154 |
| A | ALA155 |
| A | LEU159 |
| A | SER273 |
| A | PHE274 |
| A | TRP298 |
| A | GLN352 |
| A | PHE357 |
| A | LEU371 |
| A | HOH714 |
| A | PHE110 |
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 | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18784071","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10037","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18784071","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
