3ddc

Crystal Structure of NORE1A in Complex with RAS

Method: X-RAY DIFFRACTION Dmax: 72.0 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–166 Fragment:UNP residues 1-166 Mutation:D30E, E31K Ras association domain-containing family protein 5 × 2 (Q5EBH1) MG MAGNESIUM ION × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;100MM C2H3NAO2, 20% PEG 2000, 250MM (NH4)2SO4, 10MM DTE, pH 4.50, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–166 Fragment:UNP residues 1-166 Mutation:D30E, E31K Ras association domain-containing family protein 5 × 1 (Q5EBH1) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;100MM C2H3NAO2, 20% PEG 2000, 250MM (NH4)2SO4, 10MM DTE, pH 4.50, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.230

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 323 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 1–166; UniProt 1–166

Ras association domain-containing family protein 5

Mus musculus

UniProt Q5EBH1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 200–357 Fragment:RAS BINDING DOMAIN, UNP RESIDUES 200-358 Mutation:L285M, K302D GTPase HRas × 2 (P01112) MG MAGNESIUM ION × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;100MM C2H3NAO2, 20% PEG 2000, 250MM (NH4)2SO4, 10MM DTE, pH 4.50, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 200–357 Fragment:RAS BINDING DOMAIN, UNP RESIDUES 200-358 Mutation:L285M, K302D GTPase HRas × 1 (P01112) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;293 K;100MM C2H3NAO2, 20% PEG 2000, 250MM (NH4)2SO4, 10MM DTE, pH 4.50, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.80 Å R-free 0.230

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RASF5_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–163; UniProt 200–357

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 3ddc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ddc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ddc
Deposition date deposition_date2008-06-05
Structure title titleCrystal Structure of NORE1A in Complex with RAS
Keywords keywords;Oncogene, Tumorsuppressor, Ubiquitin Fold, RAS effector, RAP1, H-RAS, RASSF1, RASSF5, RAPL, NORE1, GMPPNP, Adaptor, Apoptosis, Microtubules, HYDROLASE-APOPTOSIS COMPLEX, Disease mutation, Golgi apparatus, GTP-binding, Lipoprotein, Membrane, Methylation, Nucleotide-binding, Palmitate, Prenylation, Proto-oncogene, Anti-oncogene, Cell cycle, Metal-binding, Microtubule, Phorbol-ester binding, Zinc-finger ;; HYDROLASE/APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.50
Radius of gyration Rg (electron density) rg_electron20.52
Forward intensity I(0) i020901300.00
Molecular weight molecular_weight34584.0 kDa
Excluded volume excluded_volume43291 ų
Envelope volume envelope_volume51600 ų
Hydration-shell volume shell_volume21134 ų
Envelope diameter envelope_diameter72.8
Shell Rg shell_rg27.06
Envelope Rg envelope_rg20.82
Shape Rg shape_rg20.54
Total Rg total_rg21.35
Total atoms total_atoms2427
Residues n_residues299
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 dmax72.0
Rg (real space) rg_real21.45
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real2.0900e+07
I(0) uncertainty (real space) i0_real_error2.9040e+05
Rg (reciprocal space) rg_reciprocal21.46
I(0) (reciprocal space) i0_reciprocal20900000.0000
Solution quality estimate total_estimate0.8807
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.359
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3591000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3ddca_
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 (2 domains)

Domain ID domain_id3ddcA00
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_id3ddcB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)