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1BP1

CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN

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 Residues18
DetailsBINDING SITE FOR RESIDUE PC1 A 777
ChainResidue
ASER181
ALYS185
ALEU186
ATYR189
APHE190
ALEU193
AVAL254
APRO428
APRO430
AARG432
ATYR455
AVAL7
AILE9
AALA17
AGLN20
AGLY21
AALA24
AILE68

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PC1 A 778
ChainResidue
ASER201
APHE263
AALA266
ATYR270
ALEU276
APRO324
APHE335
APRO337
ATHR362
AVAL368
ALEU375
AVAL417
ALYS420
APHE425

site_idC
Number of Residues1
DetailsAPOLAR POCKET PRIMARILY IN C-TERMINAL DOMAIN OF PROTEIN WHICH HOLDS ONE PHOSPHATIDYLCHOLINE MOLECULE.
ChainResidue
ALYS456

site_idN
Number of Residues1
DetailsAPOLAR POCKET PRIMARILY IN N-TERMINAL DOMAIN OF PROTEIN WHICH HOLDS ONE PHOSPHATIDYLCHOLINE MOLECULE.
ChainResidue
AVAL1

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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