3wam

Crystal structure of human LC3C_8-125

Method: X-RAY DIFFRACTION Dmax: 47.0 Å Quality: GOOD

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

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 8–125 Fragment:UNP RESIDUES 8-125 CIT CITRIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;0.5M di-Ammonium hydrogen citrate, 10% PEG 3350, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.75 Å R-free 0.211
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 8–125 Fragment:UNP RESIDUES 8-125 CIT CITRIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;0.5M di-Ammonium hydrogen citrate, 10% PEG 3350, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.75 Å R-free 0.211

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 3–120; 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 3wam

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3wam
Deposition date deposition_date2013-05-06
Structure title titleCrystal structure of 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_guinier15.17
Radius of gyration Rg (electron density) rg_electron13.74
Forward intensity I(0) i03528450.00
Molecular weight molecular_weight13687.0 kDa
Excluded volume excluded_volume17391 ų
Envelope volume envelope_volume19415 ų
Hydration-shell volume shell_volume11989 ų
Envelope diameter envelope_diameter44.1
Shell Rg shell_rg19.46
Envelope Rg envelope_rg14.06
Shape Rg shape_rg13.73
Total Rg total_rg15.02
Total atoms total_atoms963
Residues n_residues115
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 dmax47.0
Rg (real space) rg_real15.05
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real3.5280e+06
I(0) uncertainty (real space) i0_real_error3.7340e+04
Rg (reciprocal space) rg_reciprocal15.06
I(0) (reciprocal space) i0_reciprocal3528000.0000
Solution quality estimate total_estimate0.8963
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.406
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha751600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3wama_
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.15.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id3wamA00
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)