8t4t

Crystal structure of LC3A in complex with the LIR of TP53INP2/DOR

Method: X-RAY DIFFRACTION Dmax: 97.1 Å Quality: GOOD

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

Tumor protein p53-inducible nuclear protein 2,Microtubule-associated proteins 1A/1B light chain 3A chimera

Homo sapiens

UniProt Q8IXH6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 29–39 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;12.5% PEG3350, 0.2M NH4-citrate, 5% isopropanol, 0.1M MES pH6.5 Resolution 2.36 Å R-free 0.272
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 29–39 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;12.5% PEG3350, 0.2M NH4-citrate, 5% isopropanol, 0.1M MES pH6.5 Resolution 2.36 Å R-free 0.272

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.

5 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name T53I2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–13; UniProt 29–39 Author chain B; PDBConstruct 3–13; UniProt 29–39

Tumor protein p53-inducible nuclear protein 2,Microtubule-associated proteins 1A/1B light chain 3A chimera

Homo sapiens

UniProt Q9H492

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–121 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;12.5% PEG3350, 0.2M NH4-citrate, 5% isopropanol, 0.1M MES pH6.5 Resolution 2.36 Å R-free 0.272
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–121 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;12.5% PEG3350, 0.2M NH4-citrate, 5% isopropanol, 0.1M MES pH6.5 Resolution 2.36 Å R-free 0.272

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.

13 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLP3A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–134; UniProt 1–121 Author chain B; PDBConstruct 14–134; UniProt 1–121

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 8t4t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t4t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t4t
Deposition date deposition_date2023-06-10
Structure title titleCrystal structure of LC3A in complex with the LIR of TP53INP2/DOR
Keywords keywordsLC3A, Autophagy, DOR LIR, TP53INP2 LIR, 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_guinier23.50
Radius of gyration Rg (electron density) rg_electron22.65
Forward intensity I(0) i014976100.00
Molecular weight molecular_weight29331.0 kDa
Excluded volume excluded_volume36956 ų
Envelope volume envelope_volume49643 ų
Hydration-shell volume shell_volume19410 ų
Envelope diameter envelope_diameter100.4
Shell Rg shell_rg27.69
Envelope Rg envelope_rg23.49
Shape Rg shape_rg22.68
Total Rg total_rg23.33
Total atoms total_atoms2065
Residues n_residues249
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 dmax97.1
Rg (real space) rg_real23.61
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real1.4980e+07
I(0) uncertainty (real space) i0_real_error2.0700e+05
Rg (reciprocal space) rg_reciprocal23.59
I(0) (reciprocal space) i0_reciprocal14980000.0000
Solution quality estimate total_estimate0.7545
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis0.102
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2453000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.438; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.502; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)