2r17

Functional architecture of the retromer cargo-recognition complex

Method: X-RAY DIFFRACTION Dmax: 122.1 Å Quality: GOOD

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

Vacuolar protein sorting-associated protein 29

Homo sapiens

UniProt Q9UBQ0

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–182 Non-standard monomer:Yes (specific site not provided by mmCIF) Vacuolar protein sorting-associated protein 35 × 1 (Q96QK1) X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop;pH 8;291 K;20% PEG 3350, 1M NaCl,50mM Tris, pH 8.0, hanging drop, temperature 291K Resolution 2.80 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–182 Non-standard monomer:Yes (specific site not provided by mmCIF) Vacuolar protein sorting-associated protein 35 × 1 (Q96QK1) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop;pH 8;291 K;20% PEG 3350, 1M NaCl,50mM Tris, pH 8.0, hanging drop, temperature 291K Resolution 2.80 Å R-free 0.268

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.

20 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS29_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–183; UniProt 1–182 Author chain B; PDBConstruct 2–183; UniProt 1–182

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 483–780 Non-standard monomer:Yes (specific site not provided by mmCIF) Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop;pH 8;291 K;20% PEG 3350, 1M NaCl,50mM Tris, pH 8.0, hanging drop, temperature 291K Resolution 2.80 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 483–780 Non-standard monomer:Yes (specific site not provided by mmCIF) Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop;pH 8;291 K;20% PEG 3350, 1M NaCl,50mM Tris, pH 8.0, hanging drop, temperature 291K Resolution 2.80 Å R-free 0.268

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 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS35_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–298; UniProt 483–780 Author chain D; PDBConstruct 1–298; UniProt 483–780

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 2r17

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2r17
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2r17
Deposition date deposition_date2007-08-22
Structure title titleFunctional architecture of the retromer cargo-recognition complex
Keywords keywordsProtein Transport, Membrane, Phosphorylation; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.30
Radius of gyration Rg (electron density) rg_electron37.59
Forward intensity I(0) i0174772000.00
Molecular weight molecular_weight108450.0 kDa
Excluded volume excluded_volume136150 ų
Envelope volume envelope_volume174580 ų
Hydration-shell volume shell_volume40894 ų
Envelope diameter envelope_diameter128.9
Shell Rg shell_rg40.75
Envelope Rg envelope_rg37.65
Shape Rg shape_rg37.57
Total Rg total_rg37.88
Total atoms total_atoms7591
Residues n_residues924
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 dmax122.1
Rg (real space) rg_real37.72
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.7480e+08
I(0) uncertainty (real space) i0_real_error3.2680e+06
Rg (reciprocal space) rg_reciprocal37.47
I(0) (reciprocal space) i0_reciprocal174700000.0000
Solution quality estimate total_estimate0.8001
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.0
Skewness Skewness skewness0.550
Kurtosis Kurtosis kurtosis-0.419
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38920000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.770; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.860; Smooth: 0.227

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2r17a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.159 — Metallo-dependent phosphatases
Superfamily Superfamily superfamilyd.159.1 — Metallo-dependent phosphatases
Family Family familyd.159.1.7 — YfcE-like
Domain ID domain_idd2r17b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.159 — Metallo-dependent phosphatases
Superfamily Superfamily superfamilyd.159.1 — Metallo-dependent phosphatases
Family Family familyd.159.1.7 — YfcE-like

CATH v4.4 (4 domains)

Domain ID domain_id2r17A00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id2r17B00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id2r17C00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily660 — Vacuolar protein sorting-associated protein 35, helical subcomplex Vps35-C
Domain ID domain_id2r17D00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily660 — Vacuolar protein sorting-associated protein 35, helical subcomplex Vps35-C

8. Citations (1)

9. Files and Curves (10)