3wap

Crystal structure of Atg13 LIR-fused human LC3C_8-125

Method: X-RAY DIFFRACTION Dmax: 54.3 Å Quality: GOOD

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

Autophagy-related protein 13, Microtubule-associated proteins 1A/1B light chain 3C

Homo sapiens

UniProt O75143

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 436–447 Fragment:UNP RESIDUES 436-447, 8-125 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;277 K;0.1M Sodium acetate trihydrate, 8% PEG 4000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.10 Å R-free 0.273
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 436–447 Fragment:UNP RESIDUES 436-447, 8-125 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;277 K;0.1M Sodium acetate trihydrate, 8% PEG 4000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.10 Å R-free 0.273

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 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ATG13_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–14; UniProt 436–447

Autophagy-related protein 13, Microtubule-associated proteins 1A/1B light chain 3C

Homo sapiens

UniProt Q9BXW4

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 8–125 Fragment:UNP RESIDUES 436-447, 8-125 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;277 K;0.1M Sodium acetate trihydrate, 8% PEG 4000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.10 Å R-free 0.273
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 8–125 Fragment:UNP RESIDUES 436-447, 8-125 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;277 K;0.1M Sodium acetate trihydrate, 8% PEG 4000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 3.10 Å R-free 0.273

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.

4 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLP3C_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–134; UniProt 8–125

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 3wap

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3wap
Deposition date deposition_date2013-05-06
Structure title titleCrystal structure of Atg13 LIR-fused human LC3C_8-125
Keywords keywordsUBIQUITIN-LIKE FOLD, AUTOPHAGY, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.84
Radius of gyration Rg (electron density) rg_electron14.71
Forward intensity I(0) i03846100.00
Molecular weight molecular_weight14413.0 kDa
Excluded volume excluded_volume18384 ų
Envelope volume envelope_volume21235 ų
Hydration-shell volume shell_volume12496 ų
Envelope diameter envelope_diameter54.7
Shell Rg shell_rg20.17
Envelope Rg envelope_rg15.11
Shape Rg shape_rg14.70
Total Rg total_rg15.96
Total atoms total_atoms1014
Residues n_residues124
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 dmax54.3
Rg (real space) rg_real15.77
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.8460e+06
I(0) uncertainty (real space) i0_real_error4.4660e+04
Rg (reciprocal space) rg_reciprocal15.78
I(0) (reciprocal space) i0_reciprocal3846000.0000
Solution quality estimate total_estimate0.7802
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.222
Kurtosis Kurtosis kurtosis-0.192
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha800500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3wapa_
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 (1 domains)

Domain ID domain_id3wapA00
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)