2uzi

Crystal structure of HRAS(G12V) - anti-RAS Fv complex

Method: X-RAY DIFFRACTION Dmax: 76.4 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 × 5 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:PROTEIN WAS CRYSTALLIZED FROM 17-18 % PEG3350, 400 MM ZINC ACETATE, 100 MM SODIUM CACODYLATE, PH 5.8, 0.03 % DICHLOROMETHANE Resolution 2.00 Å R-free 0.271

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 2uzi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2uzi
Deposition date deposition_date2007-04-27
Structure title titleCrystal structure of HRAS(G12V) - anti-RAS Fv complex
Keywords keywords;SIGNAL TRANSDUCTION, IMMUNOGLOBULIN DOMAIN, MEMBRANE, ANTIBODY, ONCOGENE, PALMITATE, INTRABODY, DISEASE MUTATION, NUCLEOTIDE-BINDING, PROTO-ONCOGENE, CANCER THERAPY, GOLGI APPARATUS, PRENYLATION, METHYLATION, LIPOPROTEIN, GTP- BINDING, SIGNALING PROTEIN/IMMUNE SYSTEM, SIGNALING PROTEIN-IMMUNE SYSTEM complex ;; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.56
Radius of gyration Rg (electron density) rg_electron22.72
Forward intensity I(0) i034637200.00
Molecular weight molecular_weight43606.0 kDa
Excluded volume excluded_volume53755 ų
Envelope volume envelope_volume62610 ų
Hydration-shell volume shell_volume23422 ų
Envelope diameter envelope_diameter78.7
Shell Rg shell_rg29.37
Envelope Rg envelope_rg22.92
Shape Rg shape_rg22.69
Total Rg total_rg23.57
Total atoms total_atoms3041
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 dmax76.4
Rg (real space) rg_real23.56
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real3.4640e+07
I(0) uncertainty (real space) i0_real_error4.9730e+05
Rg (reciprocal space) rg_reciprocal23.56
I(0) (reciprocal space) i0_reciprocal34640000.0000
Solution quality estimate total_estimate0.8912
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.356
Kurtosis Kurtosis kurtosis-0.370
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6773000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.909

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_idd2uzih_
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_idd2uzil_
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_idd2uzir_
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_id2uziH00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2uziL00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id2uziR00
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 (1)

9. Files and Curves (10)