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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
ChainGOidnamespacecontents
A0003847molecular_function1-alkyl-2-acetylglycerophosphocholine esterase activity
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005576cellular_componentextracellular region
A0009395biological_processphospholipid catabolic process
A0016486biological_processpeptide hormone processing
A0016787molecular_functionhydrolase activity
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0034362cellular_componentlow-density lipoprotein particle
A0034364cellular_componenthigh-density lipoprotein particle
A0034374biological_processlow-density lipoprotein particle remodeling
A0034440biological_processlipid oxidation
A0034441biological_processplasma lipoprotein particle oxidation
A0034638biological_processphosphatidylcholine catabolic process
A0046469biological_processplatelet activating factor metabolic process
A0047499molecular_functioncalcium-independent phospholipase A2 activity
A0050729biological_processpositive regulation of inflammatory response
A0062234biological_processplatelet activating factor catabolic process
A0090026biological_processpositive regulation of monocyte chemotaxis
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 501
ChainResidue
APHE322
AHIS351
AHOH927

site_idAC2
Number of Residues5
Detailsbinding site for residue CL A 502
ChainResidue
AARG92
ALEU93
APRO325
AALA326
AHOH878

site_idAC3
Number of Residues15
Detailsbinding site for residue 71H A 503
ChainResidue
ALEU111
ALEU121
AGLY152
ALEU153
AGLY154
AALA155
ALEU159
ASER273
APHE274
ATRP298
AGLN352
APHE357
ALEU371
AHOH714
APHE110

Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. IAVIGHSFGG
ChainResidueDetails
AILE267-GLY276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:18784071
ChainResidueDetails
ASER273

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:18784071
ChainResidueDetails
AASP296
AHIS351

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN423

226707

PDB entries from 2024-10-30

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