5d94

Crystal structure of LC3-LIR peptide complex

Method: X-RAY DIFFRACTION Dmax: 50.2 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–125 Not recorded Peptide from FYVE and coiled-coil domain-containing protein 1 × 1 (Q9BQS8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1M Potassium thiocyanate, 30%(w/v) Polyethylene glycol monomethyl ether 2000 Resolution 1.53 Å R-free 0.215

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 6–130; UniProt 1–125

Peptide from FYVE and coiled-coil domain-containing protein 1

OrganismNot specified

UniProt Q9BQS8

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 B; UniProt 1276–1288 Not recorded Microtubule-associated proteins 1A/1B light chain 3B × 1 (Q9GZQ8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1M Potassium thiocyanate, 30%(w/v) Polyethylene glycol monomethyl ether 2000 Resolution 1.53 Å R-free 0.215

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FYCO1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–13; UniProt 1276–1288

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 5d94

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5d94
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5d94
Deposition date deposition_date2015-08-18
Structure title titleCrystal structure of LC3-LIR peptide complex
Keywords keywordsFYCO1, autophagy, LC3, LIR, PROTEIN BINDING-PEPTIDE complex; PROTEIN BINDING/PEPTIDE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.94
Radius of gyration Rg (electron density) rg_electron14.43
Forward intensity I(0) i04458430.00
Molecular weight molecular_weight15401.0 kDa
Excluded volume excluded_volume19497 ų
Envelope volume envelope_volume21910 ų
Hydration-shell volume shell_volume12896 ų
Envelope diameter envelope_diameter48.8
Shell Rg shell_rg20.18
Envelope Rg envelope_rg14.72
Shape Rg shape_rg14.40
Total Rg total_rg15.71
Total atoms total_atoms1085
Residues n_residues131
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 dmax50.2
Rg (real space) rg_real15.83
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real4.4580e+06
I(0) uncertainty (real space) i0_real_error4.8620e+04
Rg (reciprocal space) rg_reciprocal15.84
I(0) (reciprocal space) i0_reciprocal4458000.0000
Solution quality estimate total_estimate0.8889
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.5
Skewness Skewness skewness0.095
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha823200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5d94A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)