3x0w

Crystal structure of PLEKHM1 LIR-fused human LC3B_2-119

Method: X-RAY DIFFRACTION Dmax: 79.8 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 2–119 Fragment:UNP RESIDUES 2-119 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;0.1M Acetate, pH 5.0, 1.4M Ammonium Sulfate, 0.1M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.71 Å R-free 0.294
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–119 Fragment:UNP RESIDUES 2-119 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;0.1M Acetate, pH 5.0, 1.4M Ammonium Sulfate, 0.1M NaCl, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.71 Å R-free 0.294

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 17–134; UniProt 2–119 Author chain B; PDBConstruct 17–134; UniProt 2–119

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 3x0w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3x0w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3x0w
Deposition date deposition_date2014-10-22
Structure title titleCrystal structure of PLEKHM1 LIR-fused human LC3B_2-119
Keywords keywordsUBIQUITIN-LIKE FOLD, AUTOPHAGY, PLEKHM1, 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_guinier21.65
Radius of gyration Rg (electron density) rg_electron20.70
Forward intensity I(0) i014480100.00
Molecular weight molecular_weight28969.0 kDa
Excluded volume excluded_volume36537 ų
Envelope volume envelope_volume47551 ų
Hydration-shell volume shell_volume19596 ų
Envelope diameter envelope_diameter80.0
Shell Rg shell_rg26.39
Envelope Rg envelope_rg21.07
Shape Rg shape_rg20.72
Total Rg total_rg21.51
Total atoms total_atoms2043
Residues n_residues247
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 dmax79.8
Rg (real space) rg_real21.58
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.4480e+07
I(0) uncertainty (real space) i0_real_error1.9370e+05
Rg (reciprocal space) rg_reciprocal21.59
I(0) (reciprocal space) i0_reciprocal14480000.0000
Solution quality estimate total_estimate0.8414
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.257
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2056000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.674; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.915; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3x0wa1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.3 — GABARAP-like
Domain ID domain_idd3x0wa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3x0wb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.3 — GABARAP-like
Domain ID domain_idd3x0wb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3x0wA00
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
Domain ID domain_id3x0wB00
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)