5lpn

Structure of human Rab10 in complex with the bMERB domain of Mical-1

Method: X-RAY DIFFRACTION Dmax: 93.7 Å Quality: GOOD

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

Ras-related protein Rab-10

Homo sapiens

UniProt P61026

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–175 Chain C; UniProt 1–175 Not recorded Protein-methionine sulfoxide oxidase MICAL1 × 1 (Q8TDZ2) MG MAGNESIUM ION × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;6%-10% PEG8000 0.1M Imidazole Resolution 2.80 Å R-free 0.287

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAB10_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–177; UniProt 1–175 Author chain C; PDBConstruct 3–177; UniProt 1–175

Protein-methionine sulfoxide oxidase MICAL1

Homo sapiens

UniProt Q8TDZ2

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 918–1067 Fragment:UNP residues 918-1067 Ras-related protein Rab-10 × 2 (P61026) MG MAGNESIUM ION × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;6%-10% PEG8000 0.1M Imidazole Resolution 2.80 Å R-free 0.287

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.

10 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MICA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–153; UniProt 918–1067

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 5lpn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5lpn
Deposition date deposition_date2016-08-14
Structure title titleStructure of human Rab10 in complex with the bMERB domain of Mical-1
Keywords keywordsMical-1, DUF3585, Mical, Rab effector, Rab10, oxidoreductase, endocytosis; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.87
Radius of gyration Rg (electron density) rg_electron28.02
Forward intensity I(0) i048309100.00
Molecular weight molecular_weight53322.0 kDa
Excluded volume excluded_volume66519 ų
Envelope volume envelope_volume84791 ų
Hydration-shell volume shell_volume26465 ų
Envelope diameter envelope_diameter98.4
Shell Rg shell_rg33.65
Envelope Rg envelope_rg27.83
Shape Rg shape_rg27.99
Total Rg total_rg28.69
Total atoms total_atoms3743
Residues n_residues470
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 dmax93.7
Rg (real space) rg_real29.00
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real4.8310e+07
I(0) uncertainty (real space) i0_real_error7.8860e+05
Rg (reciprocal space) rg_reciprocal28.95
I(0) (reciprocal space) i0_reciprocal48310000.0000
Solution quality estimate total_estimate0.8687
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.3
Skewness Skewness skewness0.399
Kurtosis Kurtosis kurtosis-0.603
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8239000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.839; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.833; Smooth: 0.939

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5lpna_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches
Domain ID domain_idd5lpnc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id5lpnA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5lpnC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)