5f0l

Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1

Method: X-RAY DIFFRACTION Dmax: 152.2 Å Quality: GOOD

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

Vacuolar protein sorting-associated protein 35

Homo sapiens

UniProt Q96QK1

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 14–470 Fragment:Residues 14-470 Vacuolar protein sorting-associated protein 26A × 1 (O75436) Sorting nexin-3 × 1 (O60493) Natural resistance-associated macrophage protein 2 × 1 (P49281) SO4 SULFATE ION × 10 GOL GLYCEROL × 6 EDO 1,2-ETHANEDIOL × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;291 K;0.75 M AmSO4, 0.1 M MES pH 6.0, 15% Glycerol Resolution 3.20 Å R-free 0.259

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.

12 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS35_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–462; UniProt 14–470

Vacuolar protein sorting-associated protein 26A

Homo sapiens

UniProt O75436

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 B; UniProt 1–317 Not recorded Vacuolar protein sorting-associated protein 35 × 1 (Q96QK1) Sorting nexin-3 × 1 (O60493) Natural resistance-associated macrophage protein 2 × 1 (P49281) SO4 SULFATE ION × 10 GOL GLYCEROL × 6 EDO 1,2-ETHANEDIOL × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;291 K;0.75 M AmSO4, 0.1 M MES pH 6.0, 15% Glycerol Resolution 3.20 Å R-free 0.259

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP26A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–317; UniProt 1–317

Sorting nexin-3

Homo sapiens

UniProt O60493

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 C; UniProt 1–162 Fragment:Residues 14-470 Vacuolar protein sorting-associated protein 35 × 1 (Q96QK1) Vacuolar protein sorting-associated protein 26A × 1 (O75436) Natural resistance-associated macrophage protein 2 × 1 (P49281) SO4 SULFATE ION × 10 GOL GLYCEROL × 6 EDO 1,2-ETHANEDIOL × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;291 K;0.75 M AmSO4, 0.1 M MES pH 6.0, 15% Glycerol Resolution 3.20 Å R-free 0.259

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.

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SNX3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–167; UniProt 1–162

Natural resistance-associated macrophage protein 2

Homo sapiens

UniProt P49281

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 D; UniProt 545–568 Fragment:UNP residues 545-568 Vacuolar protein sorting-associated protein 35 × 1 (Q96QK1) Vacuolar protein sorting-associated protein 26A × 1 (O75436) Sorting nexin-3 × 1 (O60493) SO4 SULFATE ION × 10 GOL GLYCEROL × 6 EDO 1,2-ETHANEDIOL × 18 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;291 K;0.75 M AmSO4, 0.1 M MES pH 6.0, 15% Glycerol Resolution 3.20 Å R-free 0.259

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NRAM2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–24; UniProt 545–568

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 5f0l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5f0l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5f0l
Deposition date deposition_date2015-11-27
Structure title titleStructure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1
Keywords keywordsprotein transport, retromer, sorting nexin; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.52
Radius of gyration Rg (electron density) rg_electron40.15
Forward intensity I(0) i0177899000.00
Molecular weight molecular_weight108890.0 kDa
Excluded volume excluded_volume136940 ų
Envelope volume envelope_volume188550 ų
Hydration-shell volume shell_volume43339 ų
Envelope diameter envelope_diameter162.4
Shell Rg shell_rg40.44
Envelope Rg envelope_rg41.22
Shape Rg shape_rg40.17
Total Rg total_rg40.09
Total atoms total_atoms7638
Residues n_residues917
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 dmax152.2
Rg (real space) rg_real40.09
Rg uncertainty (real space) rg_real_error1.75
I(0) (real space) i0_real1.7790e+08
I(0) uncertainty (real space) i0_real_error3.1800e+06
Rg (reciprocal space) rg_reciprocal39.73
I(0) (reciprocal space) i0_reciprocal177800000.0000
Solution quality estimate total_estimate0.7860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.663
Kurtosis Kurtosis kurtosis0.295
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22220000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.596; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.584; Smooth: 0.843

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id5f0lB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily640
Domain ID domain_id5f0lB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily640
Domain ID domain_id5f0lC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1520 — PX Domain
Homologous superfamily homologous superfamily10 — Phox-like domain

8. Citations (1)

9. Files and Curves (10)