8q53

Crystal structure of truncated human Microtubule-associated proteins 1A/1B light chain 3B (MAP1LC3B) in apo form

Method: X-RAY DIFFRACTION Dmax: 51.0 Å Quality: GOOD

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

Microtubule-associated proteins 1A/1B light chain 3B

Homo sapiens

UniProt Q9GZQ8

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 1–125 Mutation:Truncation after Gly120 EDO 1,2-ETHANEDIOL × 9 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.7;293 K;36% PEG 8000, 0.1M acetate pH 4.7 Resolution 1.36 Å R-free 0.210

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.

49 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLP3B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–126; UniProt 1–125

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 8q53

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8q53
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8q53
Deposition date deposition_date2023-08-08
最后修订 last_revision2024-08-21
Structure title titleCrystal structure of truncated human Microtubule-associated proteins 1A/1B light chain 3B (MAP1LC3B) in apo form
Keywords keywordsautophagy, SGC, Structural Genomics, Structural Genomics Consortium, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.72
Radius of gyration Rg (electron density) rg_electron14.10
Forward intensity I(0) i03863870.00
Molecular weight molecular_weight14117.0 kDa
Excluded volume excluded_volume17874 ų
Envelope volume envelope_volume20212 ų
Hydration-shell volume shell_volume12251 ų
Envelope diameter envelope_diameter50.3
Shell Rg shell_rg19.83
Envelope Rg envelope_rg14.39
Shape Rg shape_rg14.09
Total Rg total_rg15.39
Total atoms total_atoms991
Residues n_residues115
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 dmax51.0
Rg (real space) rg_real15.62
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real3.8640e+06
I(0) uncertainty (real space) i0_real_error4.4280e+04
Rg (reciprocal space) rg_reciprocal15.63
I(0) (reciprocal space) i0_reciprocal3864000.0000
Solution quality estimate total_estimate0.8088
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.3
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.341
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha727100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)