3eci

Microtubule-associated protein 1 light chain 3 alpha isoform A (MAP1ALC3)

Method: X-RAY DIFFRACTION Dmax: 66.0 Å Quality: REASONABLE

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

Microtubule-associated protein 1 light chain 3 alpha

Homo sapiens

UniProt Q9H492

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 1–121 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;298 K;32 % PEG 4000, 0.1 M NA ACETATE, PH 4.50, 0.2 M AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, CRYOPROTECTION 20% GLYCEROL, TEMPERATURE 298K Resolution 2.65 Å R-free 0.304
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–121 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;298 K;32 % PEG 4000, 0.1 M NA ACETATE, PH 4.50, 0.2 M AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, CRYOPROTECTION 20% GLYCEROL, TEMPERATURE 298K Resolution 2.65 Å R-free 0.304

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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLP3A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–122; UniProt 1–121 Author chain B; PDBConstruct 2–122; UniProt 1–121

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 3eci

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3eci
Deposition date deposition_date2008-08-30
Structure title titleMicrotubule-associated protein 1 light chain 3 alpha isoform A (MAP1ALC3)
Keywords keywords;UBIQUITIN-LIKE (UB ROLL), AUTOPHAGY, CYTOPLASM, CYTOPLASMIC VESICLE, LIPOPROTEIN, MEMBRANE, MICROTUBULE, UBL CONJUGATION PATHWAY, STRUCTURAL GENOMICS CONSORTIUM, Alternative splicing, APOPTOSIS ;; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.35
Radius of gyration Rg (electron density) rg_electron19.47
Forward intensity I(0) i09321900.00
Molecular weight molecular_weight23332.0 kDa
Excluded volume excluded_volume29489 ų
Envelope volume envelope_volume36362 ų
Hydration-shell volume shell_volume16381 ų
Envelope diameter envelope_diameter63.9
Shell Rg shell_rg24.52
Envelope Rg envelope_rg19.27
Shape Rg shape_rg19.49
Total Rg total_rg20.20
Total atoms total_atoms1649
Residues n_residues224
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 dmax66.0
Rg (real space) rg_real20.30
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real9.3220e+06
I(0) uncertainty (real space) i0_real_error1.4130e+05
Rg (reciprocal space) rg_reciprocal20.31
I(0) (reciprocal space) i0_reciprocal9322000.0000
Solution quality estimate total_estimate0.6528
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.5
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1446000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 0.988; Sysdev: 0.319; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3ecia_
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_idd3ecib_
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_id3eciA00
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_id3eciB00
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)