2n46

EC-NMR Structure of Human H-RasT35S mutant protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data

Method: SOLUTION NMR Dmax: 46.9 Å Quality: EXCELLENT

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

GTPase HRas

Homo sapiens

UniProt P01112

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 1–166 Mutation:T35S No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

242 other PDB entries and 324 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RASH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–172; UniProt 1–166

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 2n46

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n46
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2n46
Deposition date deposition_date2015-06-17
Structure title titleEC-NMR Structure of Human H-RasT35S mutant protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data
Keywords keywords;EC-NMR, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, Protein Structure Initiative, PSI-Biology, Structural Genomics, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.90
Radius of gyration Rg (electron density) rg_electron15.31
Forward intensity I(0) i02079140000.00
Molecular weight molecular_weight376620.0 kDa
Excluded volume excluded_volume466600 ų
Envelope volume envelope_volume37544 ų
Hydration-shell volume shell_volume18355 ų
Envelope diameter envelope_diameter53.9
Shell Rg shell_rg23.40
Envelope Rg envelope_rg16.84
Shape Rg shape_rg15.28
Total Rg total_rg15.51
Total atoms total_atoms52220
Residues n_residues3320
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 dmax46.9
Rg (real space) rg_real15.75
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real2.0790e+09
I(0) uncertainty (real space) i0_real_error2.3620e+07
Rg (reciprocal space) rg_reciprocal15.77
I(0) (reciprocal space) i0_reciprocal2079000000.0000
Solution quality estimate total_estimate0.9032
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness-0.033
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha879600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2n46a_
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.37.1.8 — G proteins

CATH v4.4 (1 domains)

Domain ID domain_id2n46A00
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 (2)

9. Files and Curves (10)