6jpp

Solution structure of ELMO1 RBD

Method: SOLUTION NMR Dmax: 56.1 Å Quality: REASONABLE

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

Engulfment and cell motility protein 1

Homo sapiens

UniProt Q92556

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 1–113 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 100;Pressure ambient NMR sample composition:1 mM [U-100% 13C; U-100% 15N] Elmo1 RBD, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

17 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELMO1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–114; UniProt 1–113

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 6jpp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6jpp
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6jpp
Deposition date deposition_date2019-03-27
Structure title titleSolution structure of ELMO1 RBD
Keywords keywordsELMO, RAS BINDING DOMAIN, RBD, UBIQUITIN FOLD, RHOG, PROTEIN BINDING, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier20.57
Radius of gyration Rg (electron density) rg_electron20.26
Forward intensity I(0) i0944401000.00
Molecular weight molecular_weight254950.0 kDa
Excluded volume excluded_volume318520 ų
Envelope volume envelope_volume158310 ų
Hydration-shell volume shell_volume40589 ų
Envelope diameter envelope_diameter127.2
Shell Rg shell_rg38.17
Envelope Rg envelope_rg35.06
Shape Rg shape_rg20.19
Total Rg total_rg21.21
Total atoms total_atoms35820
Residues n_residues2280
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 dmax56.1
Rg (real space) rg_real18.25
Rg uncertainty (real space) rg_real_error0.15
I(0) (real space) i0_real8.9200e+08
I(0) uncertainty (real space) i0_real_error9.2120e+06
Rg (reciprocal space) rg_reciprocal21.21
I(0) (reciprocal space) i0_reciprocal944300000.0000
Solution quality estimate total_estimate0.6409
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.7
Skewness Skewness skewness0.582
Kurtosis Kurtosis kurtosis-0.138
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha1.2550
Highest regularization parameter α highest_alpha951000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.007; Oscil: 0.820; Stabil: 0.995; Sysdev: 0.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)