1bp1

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

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

BACTERICIDAL/PERMEABILITY-INCREASING PROTEIN

Homo sapiens

UniProt P17213

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BPI_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–456; UniProt 28–483

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bp1
Deposition date deposition_date1997-04-08
Structure title titleCRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN
Keywords keywordsBACTERICIDAL, PERMEABILITY-INCREASING, LIPID-BINDING, LIPOPOLYSACCHARIDE-BINDING, ANTIBIOTIC; BACTERICIDAL
Experimental Method methodX-RAY DIFFRACTION
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1bp1__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1bp1__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1bp1__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)34.37 Å
Rg (electron density)35.32 Å
Total Rg35.04 Å
Atom count3629
Residues456
Excluded volume66033 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1bp1__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bp1a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.83 — Aha1/BPI domain-like
Superfamily Superfamily superfamilyd.83.1 — Bactericidal permeability-increasing protein, BPI
Family Family familyd.83.1.1 — Bactericidal permeability-increasing protein, BPI
Domain ID domain_idd1bp1a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.83 — Aha1/BPI domain-like
Superfamily Superfamily superfamilyd.83.1 — Bactericidal permeability-increasing protein, BPI
Family Family familyd.83.1.1 — Bactericidal permeability-increasing protein, BPI

CATH v4.4 (2 domains)

Domain ID domain_id1bp1A01
Class class3 — Alpha Beta
Architecture architecture15 — Super Roll
Topology topology10 — Bactericidal permeability-increasing protein; domain 1
Homologous superfamily homologous superfamily10 — Bactericidal permeability-increasing protein; domain 1
Domain ID domain_id1bp1A02
Class class3 — Alpha Beta
Architecture architecture15 — Super Roll
Topology topology20 — Bactericidal permeability-increasing protein; domain 2
Homologous superfamily homologous superfamily10 — Bactericidal permeability-increasing protein; domain 2
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7. Citations (2)