2vh5

CRYSTAL STRUCTURE OF HRAS(G12V) - ANTI-RAS FV (disulfide free mutant) COMPLEX

Method: X-RAY DIFFRACTION Dmax: 78.5 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain R; UniProt 1–166 Fragment:RESIDUES 1-166 Mutation:YES ANTI-RAS FV HEAVY CHAIN × 1 ANTI-RAS FV LIGHT CHAIN × 1 ZN ZINC ION × 3 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.8;PROTEIN WAS CRYSTALLIZED FROM 17-18 % PEG3350, 320 MM ZINC ACETATE, 100 MM SODIUM CACODYLATE, PH 5.8, 0.03 % DICHLOROMETHANE Resolution 2.70 Å R-free 0.291

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 3
Chains and sequence ranges Author chain R; PDBConstruct 1–166; 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 2vh5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2vh5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2vh5
Deposition date deposition_date2007-11-19
Structure title titleCRYSTAL STRUCTURE OF HRAS(G12V) - ANTI-RAS FV (disulfide free mutant) COMPLEX
Keywords keywords;IMMUNOGLOBULIN DOMAIN, SIGNALING PROTEIN/IMMUNE SYSTEM, METHYLATION, PRENYLATION, LIPOPROTEIN, GTP-BINDING, SIGNAL TRANSDUCTION, NUCLEOTIDE- BINDING, DISEASE MUTATION, NUCLEOTIDE-BINDING, IMMUNE SYSTEM, MEMBRANE, ONCOGENE, ANTIBODY, PALMITATE, INTRABODY, PROTO-ONCOGENE, CANCER THERAPY, GOLGI APPARATUS ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.63
Radius of gyration Rg (electron density) rg_electron22.74
Forward intensity I(0) i033863300.00
Molecular weight molecular_weight43403.0 kDa
Excluded volume excluded_volume53717 ų
Envelope volume envelope_volume63142 ų
Hydration-shell volume shell_volume23537 ų
Envelope diameter envelope_diameter79.4
Shell Rg shell_rg29.54
Envelope Rg envelope_rg22.99
Shape Rg shape_rg22.71
Total Rg total_rg23.64
Total atoms total_atoms3039
Residues n_residues384
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 dmax78.5
Rg (real space) rg_real23.63
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real3.3860e+07
I(0) uncertainty (real space) i0_real_error4.6610e+05
Rg (reciprocal space) rg_reciprocal23.64
I(0) (reciprocal space) i0_reciprocal33860000.0000
Solution quality estimate total_estimate0.8110
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.353
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7571000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2vh5h_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2vh5l_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd2vh5r_
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 (3 domains)

Domain ID domain_id2vh5H00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2vh5L00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2vh5R00
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)