3q90

Crystal structure of the NTF2 domain of Ras GTPase-activating protein-binding protein 1

Method: X-RAY DIFFRACTION Dmax: 63.9 Å Quality: GOOD

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

Ras GTPase-activating protein-binding protein 1

Homo sapiens

UniProt Q13283

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–139 Chain B; UniProt 1–139 Fragment:unp residues 1-139 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;277 K;25% w/v PEG3350, 0.2M AMMONIUM ACETATE, 0.1M BIS-TRIS, VAPOR DIFFUSION, SITTING DROP, temperature 277K, pH 5.5 Resolution 1.70 Å R-free 0.238

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.

19 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G3BP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–140; UniProt 1–139 Author chain B; PDBConstruct 2–140; UniProt 1–139

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 3q90

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3q90
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3q90
Deposition date deposition_date2011-01-07
Structure title titleCrystal structure of the NTF2 domain of Ras GTPase-activating protein-binding protein 1
Keywords keywords;Structural Genomics, Structural Genomics Consortium, SGC, NTF2-like (a+b proteins), Protein Binding and Helicase, Protein (Ras GTPase-activating protein), DNA and RNA binding, plasma membrane, nucleus, HYDROLASE ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.70
Radius of gyration Rg (electron density) rg_electron18.25
Forward intensity I(0) i014956200.00
Molecular weight molecular_weight28575.0 kDa
Excluded volume excluded_volume35595 ų
Envelope volume envelope_volume42660 ų
Hydration-shell volume shell_volume19327 ų
Envelope diameter envelope_diameter66.8
Shell Rg shell_rg24.78
Envelope Rg envelope_rg18.82
Shape Rg shape_rg18.18
Total Rg total_rg19.44
Total atoms total_atoms2015
Residues n_residues251
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 dmax63.9
Rg (real space) rg_real19.62
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real1.4960e+07
I(0) uncertainty (real space) i0_real_error1.6210e+05
Rg (reciprocal space) rg_reciprocal19.63
I(0) (reciprocal space) i0_reciprocal14960000.0000
Solution quality estimate total_estimate0.8075
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.262
Kurtosis Kurtosis kurtosis-0.349
Angular range angular_range— – 0.4050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4366000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3q90a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.4 — NTF2-like
Family Family familyd.17.4.0 — automated matches
Domain ID domain_idd3q90b1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.4 — NTF2-like
Family Family familyd.17.4.0 — automated matches
Domain ID domain_idd3q90b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3q90A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily50
Domain ID domain_id3q90B00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily50

8. Citations (1)

9. Files and Curves (10)