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 | 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 |
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 | ACT_SITE: Nucleophile => ECO:0000269|PubMed:18784071 |
Chain | Residue | Details |
A | SER273 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:18784071 |
Chain | Residue | Details |
A | ASP296 | |
A | HIS351 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN423 |