7mp5

Autoinhibited neurofibrobmin

Method: ELECTRON MICROSCOPY Dmax: 168.5 Å Quality: GOOD

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

Isoform I of Neurofibromin

Homo sapiens

UniProt P21359

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–2818 Chain B; UniProt 2–2818 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 Å

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.

25 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NF1_HUMAN
Isoform P21359-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–2826; UniProt 2–2818 Author chain B; PDBConstruct 10–2826; UniProt 2–2818

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 7mp5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mp5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7mp5
Deposition date deposition_date2021-05-04
Structure title titleAutoinhibited neurofibrobmin
Keywords keywordsscaffold, RAS-GAP, HEAT repeat, autoinhibition, tumour suppressor, ANTITUMOR PROTEIN; ANTITUMOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.41
Radius of gyration Rg (electron density) rg_electron51.53
Forward intensity I(0) i0890072000.00
Molecular weight molecular_weight258680.0 kDa
Excluded volume excluded_volume328450 ų
Envelope volume envelope_volume478980 ų
Hydration-shell volume shell_volume80117 ų
Envelope diameter envelope_diameter178.3
Shell Rg shell_rg53.50
Envelope Rg envelope_rg49.79
Shape Rg shape_rg51.51
Total Rg total_rg51.65
Total atoms total_atoms18182
Residues n_residues2302
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 dmax168.5
Rg (real space) rg_real51.53
Rg uncertainty (real space) rg_real_error1.81
I(0) (real space) i0_real8.9010e+08
I(0) uncertainty (real space) i0_real_error1.8500e+07
Rg (reciprocal space) rg_reciprocal51.30
I(0) (reciprocal space) i0_reciprocal889800000.0000
Solution quality estimate total_estimate0.8459
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.8
Skewness Skewness skewness0.452
Kurtosis Kurtosis kurtosis-0.097
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46260000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.343

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)