4ddp

crystal structure of Beclin 1 evolutionarily conserved domain(ECD)

Method: X-RAY DIFFRACTION Dmax: 66.7 Å Quality: REASONABLE

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

Beclin-1

Homo sapiens

UniProt Q14457

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 241–450 Fragment:UNP residues 241-450 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;30% PEG 3350, 0.3M NaCl, 0.1M Tris pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.55 Å R-free 0.203

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.

29 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BECN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–210; UniProt 241–450

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 4ddp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ddp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ddp
Deposition date deposition_date2012-01-19
Structure title titlecrystal structure of Beclin 1 evolutionarily conserved domain(ECD)
Keywords keywordsBeclin 1, ECD, autophagy, membrane binding, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.18
Radius of gyration Rg (electron density) rg_electron15.89
Forward intensity I(0) i08969870.00
Molecular weight molecular_weight22495.0 kDa
Excluded volume excluded_volume28316 ų
Envelope volume envelope_volume31848 ų
Hydration-shell volume shell_volume16440 ų
Envelope diameter envelope_diameter54.8
Shell Rg shell_rg22.30
Envelope Rg envelope_rg16.30
Shape Rg shape_rg15.90
Total Rg total_rg16.97
Total atoms total_atoms3116
Residues n_residues195
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax66.7
Rg (real space) rg_real17.05
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real8.9700e+06
I(0) uncertainty (real space) i0_real_error1.1920e+05
Rg (reciprocal space) rg_reciprocal17.06
I(0) (reciprocal space) i0_reciprocal8970000.0000
Solution quality estimate total_estimate0.5679
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3333000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.434; Stabil: 1.000; Sysdev: 0.379; Positv: 1.000; Valcen: 0.942; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4ddpA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily40 — Autophagy protein 6/Beclin 1

8. Citations (1)

9. Files and Curves (10)