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1ewf

THE 1.7 ANGSTROM CRYSTAL STRUCTURE OF BPI

Method: X-RAY DIFFRACTION Dmax: 128.8 Å Quality: REASONABLE
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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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 28–483 Mutation：S351A PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.8；289 K；12 % PEG 6000, 0.2 M Mg Acetate, 0.1 M Na Cacodylate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 16K Resolution 1.70 Å R-free 0.250

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1EWF Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BP1 CRYSTAL STRUCTURE OF BPI, THE HUMAN BACTERICIDAL PERMEABILITY-INCREASING PROTEIN Deposited 1997-04-08 Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–483（456 aa）
Mutation：S351A PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.8；CRYSTALLIZED IN 12% PEG 8000, 0.2 M MG ACETATE, 0.1 NA CACODYLATE PH 6.8
Resolution 2.40 Å R-free 0.295

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1ewf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ewf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ewf
Deposition date deposition_date2000-04-25
Structure title titleTHE 1.7 ANGSTROM CRYSTAL STRUCTURE OF BPI
Keywords keywordsBACTERICIDAL, PERMEABILITY-INCREASING, LIPID-BINDING, LIPOPOLYSACCHARIDE-BINDING, ANTIBIOTIC; ANTIBIOTIC
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier34.22 Å
Radius of gyration Rg (electron density) rg_electron35.21 Å
Forward intensity I(0) i037079000.00
Molecular weight molecular_weight51393.0 kDa
Excluded volume excluded_volume65781 ų
Envelope volume envelope_volume82000 ų
Hydration-shell volume shell_volume23736 ų
Envelope diameter envelope_diameter137.0 Å
Shell Rg shell_rg33.57 Å
Envelope Rg envelope_rg35.98 Å
Shape Rg shape_rg35.25 Å
Total Rg total_rg34.96 Å
Total atoms total_atoms3618
Residues n_residues456
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax128.8 Å
Rg (real space) rg_real34.94 Å
Rg uncertainty (real space) rg_real_error1.59 Å
I(0) (real space) i0_real3.7080e+07
I(0) uncertainty (real space) i0_real_error5.6740e+05
Rg (reciprocal space) rg_reciprocal34.49 Å
I(0) (reciprocal space) i0_reciprocal37060000.0000
Solution quality estimate total_estimate0.6569
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.2 Å
Skewness Skewness skewness0.757
Kurtosis Kurtosis kurtosis-0.055
Angular range angular_range— – 0.2300 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9647000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.244; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.127; Smooth: 0.677
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ewfa1
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_idd1ewfa2
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_id1ewfA01
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_id1ewfA02
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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8. Citations (2)

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9. Files and Curves (10)