8q7k

IRGQ LIR2 peptide in complex with LC3B

Method: X-RAY DIFFRACTION Dmax: 64.5 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–125 Not recorded Immunity-related GTPase family Q protein × 1 (Q8WZA9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;293 K;1 M lithium chloride, 0.1 M citrate, 20% PEG 6000 Resolution 1.60 Å R-free 0.213
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–125 Not recorded Immunity-related GTPase family Q protein × 1 (Q8WZA9) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;293 K;1 M lithium chloride, 0.1 M citrate, 20% PEG 6000 Resolution 1.60 Å R-free 0.213

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 63 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 1–125; UniProt 1–125 Author chain B; PDBConstruct 1–125; UniProt 1–125

Immunity-related GTPase family Q protein

OrganismNot specified

UniProt Q8WZA9

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 417–425 Not recorded Microtubule-associated proteins 1A/1B light chain 3B × 1 (Q9GZQ8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;293 K;1 M lithium chloride, 0.1 M citrate, 20% PEG 6000 Resolution 1.60 Å R-free 0.213
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 417–425 Not recorded Microtubule-associated proteins 1A/1B light chain 3B × 1 (Q9GZQ8) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;293 K;1 M lithium chloride, 0.1 M citrate, 20% PEG 6000 Resolution 1.60 Å R-free 0.213

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IRGQ_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–9; UniProt 417–425 Author chain D; PDBConstruct 1–9; UniProt 417–425

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 8q7k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8q7k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8q7k
Deposition date deposition_date2023-08-16
Structure title titleIRGQ LIR2 peptide in complex with LC3B
Keywords keywordsAutophagy, LC3B, LIR, IRGQ, 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_guinier21.33
Radius of gyration Rg (electron density) rg_electron20.18
Forward intensity I(0) i015097200.00
Molecular weight molecular_weight29738.0 kDa
Excluded volume excluded_volume37462 ų
Envelope volume envelope_volume45771 ų
Hydration-shell volume shell_volume19235 ų
Envelope diameter envelope_diameter65.2
Shell Rg shell_rg26.08
Envelope Rg envelope_rg20.14
Shape Rg shape_rg20.18
Total Rg total_rg21.03
Total atoms total_atoms4197
Residues n_residues250
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 dmax64.5
Rg (real space) rg_real21.26
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.5100e+07
I(0) uncertainty (real space) i0_real_error1.9830e+05
Rg (reciprocal space) rg_reciprocal21.27
I(0) (reciprocal space) i0_reciprocal15100000.0000
Solution quality estimate total_estimate0.9152
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.207
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3060000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)