1k8r

Crystal structure of Ras-Bry2RBD complex

Method: X-RAY DIFFRACTION Dmax: 66.8 Å Quality: GOOD

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

Transforming protein P21/H-RAS-1

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–166 Fragment:GTP-binding/catalytic domain, residues 1-166 Protein kinase byr2 × 1 (P28829) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;290 K;PEG 3350, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.00 Å R-free 0.305

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 1–166; UniProt 1–166

Protein kinase byr2

Schizosaccharomyces pombe

UniProt P28829

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 71–180 Fragment:Ras binding domain (RBD), residues 71-180 Transforming protein P21/H-RAS-1 × 1 (P01112) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;290 K;PEG 3350, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.00 Å R-free 0.305

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 BYR2_SCHPO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–110; UniProt 71–180

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 1k8r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k8r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k8r
Deposition date deposition_date2001-10-25
Structure title titleCrystal structure of Ras-Bry2RBD complex
Keywords keywordssignal transduction, cancer, GTPase, ubiquitin fold, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.80
Radius of gyration Rg (electron density) rg_electron18.90
Forward intensity I(0) i015778300.00
Molecular weight molecular_weight28731.0 kDa
Excluded volume excluded_volume35534 ų
Envelope volume envelope_volume42438 ų
Hydration-shell volume shell_volume19017 ų
Envelope diameter envelope_diameter65.5
Shell Rg shell_rg24.96
Envelope Rg envelope_rg19.15
Shape Rg shape_rg18.89
Total Rg total_rg19.79
Total atoms total_atoms2012
Residues n_residues248
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 dmax66.8
Rg (real space) rg_real19.76
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real1.5780e+07
I(0) uncertainty (real space) i0_real_error1.7610e+05
Rg (reciprocal space) rg_reciprocal19.76
I(0) (reciprocal space) i0_reciprocal15780000.0000
Solution quality estimate total_estimate0.8673
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.189
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4091000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.765; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1k8ra_
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
Domain ID domain_idd1k8rb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.5 — Ras-binding domain, RBD

CATH v4.4 (2 domains)

Domain ID domain_id1k8rA00
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_id1k8rB00
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)