5cx3

Crystal structure of FYCO1 LIR in complex with LC3A

Method: X-RAY DIFFRACTION Dmax: 89.4 Å Quality: EXCELLENT

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

Microtubule-associated proteins 1A/1B light chain 3A

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–121 Chain C; UniProt 1–121 Not recorded FYVE and coiled-coil domain-containing protein 1 × 2 (Q9BQS8) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;289 K;1.2 M sodium citrate tribasic dihydrate, 0.1 M HEPES sodium Resolution 2.30 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–121 Chain D; UniProt 1–121 Not recorded FYVE and coiled-coil domain-containing protein 1 × 2 (Q9BQS8) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;289 K;1.2 M sodium citrate tribasic dihydrate, 0.1 M HEPES sodium Resolution 2.30 Å R-free 0.244
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–121 Chain B; UniProt 1–121 Chain C; UniProt 1–121 Chain D; UniProt 1–121 Not recorded FYVE and coiled-coil domain-containing protein 1 × 4 (Q9BQS8) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;289 K;1.2 M sodium citrate tribasic dihydrate, 0.1 M HEPES sodium Resolution 2.30 Å R-free 0.244

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 19 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 1–121; UniProt 1–121 Author chain B; PDBConstruct 1–121; UniProt 1–121 Author chain C; PDBConstruct 1–121; UniProt 1–121 Author chain D; PDBConstruct 1–121; UniProt 1–121

FYVE and coiled-coil domain-containing protein 1

Homo sapiens

UniProt Q9BQS8

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1273–1298 Chain G; UniProt 1273–1298 Not recorded Microtubule-associated proteins 1A/1B light chain 3A × 2 (Q9H492) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;289 K;1.2 M sodium citrate tribasic dihydrate, 0.1 M HEPES sodium Resolution 2.30 Å R-free 0.244
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1273–1298 Chain H; UniProt 1273–1298 Not recorded Microtubule-associated proteins 1A/1B light chain 3A × 2 (Q9H492) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;289 K;1.2 M sodium citrate tribasic dihydrate, 0.1 M HEPES sodium Resolution 2.30 Å R-free 0.244
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1273–1298 Chain F; UniProt 1273–1298 Chain G; UniProt 1273–1298 Chain H; UniProt 1273–1298 Not recorded Microtubule-associated proteins 1A/1B light chain 3A × 4 (Q9H492) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;289 K;1.2 M sodium citrate tribasic dihydrate, 0.1 M HEPES sodium Resolution 2.30 Å R-free 0.244

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FYCO1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–26; UniProt 1273–1298 Author chain F; PDBConstruct 1–26; UniProt 1273–1298 Author chain G; PDBConstruct 1–26; UniProt 1273–1298 Author chain H; PDBConstruct 1–26; UniProt 1273–1298

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 5cx3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5cx3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5cx3
Deposition date deposition_date2015-07-28
Structure title titleCrystal structure of FYCO1 LIR in complex with LC3A
Keywords keywordsautophagy adaptor, 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_guinier29.55
Radius of gyration Rg (electron density) rg_electron28.45
Forward intensity I(0) i067410000.00
Molecular weight molecular_weight64801.0 kDa
Excluded volume excluded_volume81340 ų
Envelope volume envelope_volume107240 ų
Hydration-shell volume shell_volume30754 ų
Envelope diameter envelope_diameter96.3
Shell Rg shell_rg36.58
Envelope Rg envelope_rg27.97
Shape Rg shape_rg28.43
Total Rg total_rg29.36
Total atoms total_atoms4571
Residues n_residues553
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 dmax89.4
Rg (real space) rg_real29.44
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real6.7410e+07
I(0) uncertainty (real space) i0_real_error1.1120e+06
Rg (reciprocal space) rg_reciprocal29.49
I(0) (reciprocal space) i0_reciprocal67410000.0000
Solution quality estimate total_estimate0.9098
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary44.7
Skewness Skewness skewness0.120
Kurtosis Kurtosis kurtosis-0.638
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37440000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.956; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5cx3a_
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_idd5cx3b_
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_idd5cx3c_
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_idd5cx3d_
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 (4 domains)

Domain ID domain_id5cx3A00
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_id5cx3B00
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_id5cx3C00
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_id5cx3D00
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)