1ctq

STRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP AT 100 K

Method: X-RAY DIFFRACTION Dmax: 48.6 Å Quality: REASONABLE

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

PROTEIN (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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–166 Fragment:RESIDUES 1-166 MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:MICROBATCH;pH 7.6;291 K;PROTEIN WAS CRYSTALLIZED FROM 28 % PEG 400, 10MM MGCL 264MM TRIS/HCL, PH 7.6, pH 7.60, micro-batch, temperature 18K Resolution 1.26 Å R-free 0.224

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

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 1ctq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ctq
Deposition date deposition_date1999-08-20
Structure title titleSTRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP AT 100 K
Keywords keywordsG PROTEIN, GTP HYDROLYSIS, KINETIC CRYSTALLOGRAPHY, 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_guinier16.23
Radius of gyration Rg (electron density) rg_electron14.89
Forward intensity I(0) i07821960.00
Molecular weight molecular_weight19375.0 kDa
Excluded volume excluded_volume23768 ų
Envelope volume envelope_volume26400 ų
Hydration-shell volume shell_volume14688 ų
Envelope diameter envelope_diameter47.5
Shell Rg shell_rg21.11
Envelope Rg envelope_rg15.16
Shape Rg shape_rg14.89
Total Rg total_rg15.95
Total atoms total_atoms1355
Residues n_residues166
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 dmax48.6
Rg (real space) rg_real16.08
Rg uncertainty (real space) rg_real_error0.19
I(0) (real space) i0_real7.8220e+06
I(0) uncertainty (real space) i0_real_error7.9560e+04
Rg (reciprocal space) rg_reciprocal16.09
I(0) (reciprocal space) i0_reciprocal7822000.0000
Solution quality estimate total_estimate0.7292
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.011
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1423000.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.972; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ctqa_
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_id1ctqA00
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)