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1EWF

THE 1.7 ANGSTROM CRYSTAL STRUCTURE OF BPI

Functional Information from GO Data
ChainGOidnamespacecontents
A0001530molecular_functionlipopolysaccharide binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0008289molecular_functionlipid binding
A0016020cellular_componentmembrane
A0031663biological_processlipopolysaccharide-mediated signaling pathway
A0032715biological_processnegative regulation of interleukin-6 production
A0032717biological_processnegative regulation of interleukin-8 production
A0032720biological_processnegative regulation of tumor necrosis factor production
A0035578cellular_componentazurophil granule lumen
A0035580cellular_componentspecific granule lumen
A0042742biological_processdefense response to bacterium
A0043031biological_processnegative regulation of macrophage activation
A0045087biological_processinnate immune response
A0050829biological_processdefense response to Gram-negative bacterium
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE PC1 A 577
ChainResidue
AALA17
AVAL222
AVAL254
ALEU256
ALEU427
APRO428
AARG432
ALEU435
AVAL453
ATYR455
AHOH968
AGLY21
AALA24
ASER181
AGLU185
ALEU186
ATYR189
APHE190
ALEU193

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PC1 A 578
ChainResidue
APHE263
ATYR270
ALEU276
ALYS277
ALEU326
APHE335
AMET366
AVAL368
ALEU381
AVAL417
ALYS420
APHE425

Functional Information from PROSITE/UniProt
site_idPS00400
Number of Residues33
DetailsLBP_BPI_CETP LBP / BPI / CETP family signature. PGVvvRISqkgLdyasqQgtaaLQkelkrikiP
ChainResidueDetails
APRO3-PRO35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AALA353

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PDB entries from 2024-07-24

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