5v4k

Crystal structure of NEDD4 LIR-fused human LC3B_2-119

Method: X-RAY DIFFRACTION Dmax: 84.4 Å Quality: GOOD

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

;Microtubule-associated proteins 1A/1B light chain 3B,Microtubule-associated proteins 1A/1B light chain 3B,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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–119 Chain B; UniProt 2–119 Fragment:UNP residues 2-119,UNP residues 2-119,UNP residues 2-119,UNP residues 2-119 GOL GLYCEROL × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;0.1M Sodium Acetate pH 5.0, 1.2M Ammonium Sulfate Resolution 2.10 Å R-free 0.233

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 15–132; UniProt 2–119 Author chain B; PDBConstruct 15–132; 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 5v4k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5v4k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5v4k
Deposition date deposition_date2017-03-09
Structure title titleCrystal structure of NEDD4 LIR-fused human LC3B_2-119
Keywords keywordsAutophagy, Ubiquitin E3 ligase, HECT, LIR, LC3, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.95
Radius of gyration Rg (electron density) rg_electron21.08
Forward intensity I(0) i014278600.00
Molecular weight molecular_weight28645.0 kDa
Excluded volume excluded_volume36020 ų
Envelope volume envelope_volume47332 ų
Hydration-shell volume shell_volume19340 ų
Envelope diameter envelope_diameter85.5
Shell Rg shell_rg26.51
Envelope Rg envelope_rg21.62
Shape Rg shape_rg21.10
Total Rg total_rg21.83
Total atoms total_atoms2018
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 dmax84.4
Rg (real space) rg_real21.93
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.4280e+07
I(0) uncertainty (real space) i0_real_error2.2170e+05
Rg (reciprocal space) rg_reciprocal21.94
I(0) (reciprocal space) i0_reciprocal14280000.0000
Solution quality estimate total_estimate0.8134
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.362
Kurtosis Kurtosis kurtosis0.038
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1911000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.587; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.810; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5v4ka_
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_idd5v4kb_
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

CATH v4.4 (2 domains)

Domain ID domain_id5v4kA00
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_id5v4kB00
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)