SAXSdb — 1a44

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN

OrganismNot specified

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 1–185	Not recorded	ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：pH 4.6；pH 4.6	Resolution 1.84 Å R-free 0.216

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 1A44	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B7A STRUCTURE OF THE PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN FROM BOVINE BRAIN Deposited 1999-01-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 2–187（186 aa） Chain B 2–187（186 aa）	Not recorded	OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.3；25-27% PEG8000, 100 MM PHOSPHORYLETHANOLAMINE, pH 4.3	Resolution 2.25 Å R-free 0.279

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

View Construct and Data Evidence

UniProt name	PEBP_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–185； UniProt 1–185

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1a44
Deposition date deposition_date	1998-02-10
Structure title title	PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FROM CALF BRAIN
Keywords keywords	LIPID-BINDING, LIPID-BINDING PROTEIN, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	16.57 Å
Radius of gyration Rg (electron density) rg_electron	15.26 Å
Forward intensity I(0) i0	7906190.00
Molecular weight molecular_weight	20784.0 kDa
Excluded volume excluded_volume	26050 Å³
Envelope volume envelope_volume	28446 Å³
Hydration-shell volume shell_volume	15357 Å³
Envelope diameter envelope_diameter	50.8 Å
Shell Rg shell_rg	21.65 Å
Envelope Rg envelope_rg	15.62 Å
Shape Rg shape_rg	15.23 Å
Total Rg total_rg	16.46 Å
Total atoms total_atoms	1470
Residues n_residues	185
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	52.2 Å
Rg (real space) rg_real	16.42 Å
Rg uncertainty (real space) rg_real_error	0.22 Å
I(0) (real space) i0_real	7.9060e+06
I(0) uncertainty (real space) i0_real_error	8.9100e+04
Rg (reciprocal space) rg_reciprocal	16.44 Å
I(0) (reciprocal space) i0_reciprocal	7906000.0000
Solution quality estimate total_estimate	0.8886
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	22.4 Å
Skewness Skewness skewness	0.080
Kurtosis Kurtosis kurtosis	-0.417
Angular range angular_range	— – 0.4800 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	2323000.0000
Real-space data points n_real_points	78
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.997

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (3)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1a44a_
Class class	b — All beta proteins
Fold Fold fold	b.17 — PEBP-like
Superfamily Superfamily superfamily	b.17.1 — PEBP-like
Family Family family	b.17.1.1 — Phosphatidylethanolamine binding protein

CATH v4.4 (1 domains)

Domain ID domain_id	1a44A00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	280 — Phosphatidylethanolamine-binding Protein
Homologous superfamily homologous superfamily	10 — PEBP-like

▶

8. Citations (1)

▶

Unit-cell length a length_a	82.700 Å
Unit-cell length b length_b	33.550 Å
Unit-cell length c length_c	60.070 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	97.71 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.840 Å
Low-resolution limit resolution_low	36.000 Å
R factor r_factor	—
R_work r_work	0.1480
R_free r_free	0.2160

Description description	PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN
Molecular weight formula_weight	20754.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1714

PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FROM CALF BRAIN

1. Protein Identity and Related Structures Protein Identity & Related Structures

PHOSPHATIDYLETHANOLAMINE-BINDING PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	1

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	244

fit	/app/data/saxs_computation/a4/1a44/1a44.fit
pddf	/app/data/pr_computation/a4/1a44/1a44.pr.out
profile	/app/data/saxs_computation/a4/1a44/1a44.dat