1xke

Solution structure of the second Ran-binding domain from human RanBP2

Method: SOLUTION NMR Dmax: 55.3 Å Quality: GOOD

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

Ran-binding protein 2

Homo sapiens

UniProt P49792

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 2028–2154 Fragment:Ran-binding domain 2 (RanBD2) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;298 K;Ionic strength (raw mmCIF value) 150 mM Na2SO4;Pressure ambient NMR sample composition:1.4mM RanBD2 U-13C; U-15N; 150mM Na2SO4; 10mM DTE; 0.5 mM EDTA; 1mM NaN3; 0.1mM DSS; 10mM potassium phosphate buffer at pH 6.5; | 92% H2O, 8%D2O NMR sample composition:0.7mM RanBD2 U-13C; U-15N; 150mM Na2SO4; 10mM DTE; 0.5mM EDTA; 1mM NaN3; 0.1mM DSS; 10mM potassium phosphate buffer at pH 6.5; | 100% D2O NMR sample composition:1.0mM RanBD2 U-15N; 150mM Na2SO4; 10mM DTE; 0.5mM EDTA; 1mM NaN3; 0.1 mM DSS; 10mM potassium phosphate buffer at pH 6.5; | 92% H2O, 8%D2O NMR sample composition:1.0mM RanBD2 U-15N; 150mM Na2SO4; 10mM DTE; 0.5mM EDTA; 1mM NaN3; 0.1mM DSS; 10mM potassium phosphate buffer at pH 6.5; | 100% 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.

31 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–129; UniProt 2028–2154

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 1xke

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xke
Deposition date deposition_date2004-09-28
Structure title titleSolution structure of the second Ran-binding domain from human RanBP2
Keywords keywordsbeta barrel, pleckstrin-homology (PH) domain, phosphotyrosine-binding (PTB) domain, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.52
Radius of gyration Rg (electron density) rg_electron14.30
Forward intensity I(0) i01234960000.00
Molecular weight molecular_weight302350.0 kDa
Excluded volume excluded_volume380410 ų
Envelope volume envelope_volume34374 ų
Hydration-shell volume shell_volume17015 ų
Envelope diameter envelope_diameter60.8
Shell Rg shell_rg23.30
Envelope Rg envelope_rg17.44
Shape Rg shape_rg14.28
Total Rg total_rg14.51
Total atoms total_atoms42840
Residues n_residues2600
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 dmax55.3
Rg (real space) rg_real14.45
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.2350e+09
I(0) uncertainty (real space) i0_real_error1.7750e+07
Rg (reciprocal space) rg_reciprocal14.46
I(0) (reciprocal space) i0_reciprocal1235000000.0000
Solution quality estimate total_estimate0.8069
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.122
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha381700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.520; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.928; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1xkea1
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.3 — Ran-binding domain
Domain ID domain_idd1xkea2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd1xkea3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1xkeA00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

8. Citations (2)

9. Files and Curves (10)