2n1b

NMR solution structure of nucleotide-free Ran GTPase

Method: SOLUTION NMR Dmax: 49.8 Å Quality: GOOD

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

GTP-binding nuclear protein Ran

Homo sapiens

UniProt P62826

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 1–216 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Ionic strength (raw mmCIF value) 102;Pressure ambient NMR sample composition:0.5 mM [U-100% 13C; U-100% 15N] RAN GTPASE, 20 mM HEPES, 2 mM DTT, 0.04 % sodium azide, 100 mM potassium chloride, 2 mM magnesium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

137 other PDB entries and 203 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 42–257; UniProt 1–216

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 2n1b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n1b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n1b
Deposition date deposition_date2015-03-26
Structure title titleNMR solution structure of nucleotide-free Ran GTPase
Keywords keywordsTRANSPORT PROTEIN, G PROTEIN, NUCLEOTIDE-BINDING, GTP-BINDING, NUCLEUS; TRANSPORT PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.27
Radius of gyration Rg (electron density) rg_electron16.92
Forward intensity I(0) i0777131000.00
Molecular weight molecular_weight244060.0 kDa
Excluded volume excluded_volume308570 ų
Envelope volume envelope_volume36009 ų
Hydration-shell volume shell_volume17443 ų
Envelope diameter envelope_diameter56.2
Shell Rg shell_rg23.44
Envelope Rg envelope_rg17.53
Shape Rg shape_rg16.90
Total Rg total_rg17.12
Total atoms total_atoms34470
Residues n_residues2160
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 dmax49.8
Rg (real space) rg_real17.14
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real7.7710e+08
I(0) uncertainty (real space) i0_real_error8.5860e+06
Rg (reciprocal space) rg_reciprocal17.16
I(0) (reciprocal space) i0_reciprocal777100000.0000
Solution quality estimate total_estimate0.8353
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.051
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha867800.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2n1ba_
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_id2n1bA00
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)