7cnd

NCI-1 in complex with CRM1-Ran-RanBP1

Method: X-RAY DIFFRACTION Dmax: 109.4 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–216 Mutation:Q69L, L182A YRB1 isoform 1 × 1 (A0A6A5PZB5) CRM1 isoform 1 × 1 (A0A6A5PZI8) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 DMS DIMETHYL SULFOXIDE × 6 CL CHLORIDE ION × 9 G6U ~{N}-[(~{E})-3-[3,5-bis(trifluoromethyl)phenyl]sulfinylprop-2-enyl]-3-methyl-butan-1-amine × 1 GOL GLYCEROL × 1 MPO 3[N-MORPHOLINO]PROPANE SULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.12 M Monosaccharides (20 mM D-Glucose; 20 mM D-Mannose; 20 mM D-Galactose; 20 mM L-Fucose; 20 mM D-Xylose; 20 mM N-Acetyl-D-Glucosamine), 0.1 M buffer system 1 pH 6.5 (sodium HEPES and MOPS), and 50 % Precipitant Mix 2 (40% v/v Ethylene glycol; 20 % w/v PEG 8000) Resolution 1.80 Å R-free 0.232

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 1–216; UniProt 1–216

YRB1 isoform 1

Saccharomyces cerevisiae

UniProt A0A6A5PZB5

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 62–201 Not recorded GTP-binding nuclear protein Ran × 1 (P62826) CRM1 isoform 1 × 1 (A0A6A5PZI8) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 DMS DIMETHYL SULFOXIDE × 6 CL CHLORIDE ION × 9 G6U ~{N}-[(~{E})-3-[3,5-bis(trifluoromethyl)phenyl]sulfinylprop-2-enyl]-3-methyl-butan-1-amine × 1 GOL GLYCEROL × 1 MPO 3[N-MORPHOLINO]PROPANE SULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.12 M Monosaccharides (20 mM D-Glucose; 20 mM D-Mannose; 20 mM D-Galactose; 20 mM L-Fucose; 20 mM D-Xylose; 20 mM N-Acetyl-D-Glucosamine), 0.1 M buffer system 1 pH 6.5 (sodium HEPES and MOPS), and 50 % Precipitant Mix 2 (40% v/v Ethylene glycol; 20 % w/v PEG 8000) Resolution 1.80 Å R-free 0.232

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PZB5_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–140; UniProt 62–201

CRM1 isoform 1

Saccharomyces cerevisiae

UniProt A0A6A5PZI8

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–1058 Mutation:S27E , Q49E, del377-413, del441-461, D537G, V540E, K541Q, S553R, Q561E, A741T, Y1022C GTP-binding nuclear protein Ran × 1 (P62826) YRB1 isoform 1 × 1 (A0A6A5PZB5) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 DMS DIMETHYL SULFOXIDE × 6 CL CHLORIDE ION × 9 G6U ~{N}-[(~{E})-3-[3,5-bis(trifluoromethyl)phenyl]sulfinylprop-2-enyl]-3-methyl-butan-1-amine × 1 GOL GLYCEROL × 1 MPO 3[N-MORPHOLINO]PROPANE SULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.12 M Monosaccharides (20 mM D-Glucose; 20 mM D-Mannose; 20 mM D-Galactose; 20 mM L-Fucose; 20 mM D-Xylose; 20 mM N-Acetyl-D-Glucosamine), 0.1 M buffer system 1 pH 6.5 (sodium HEPES and MOPS), and 50 % Precipitant Mix 2 (40% v/v Ethylene glycol; 20 % w/v PEG 8000) Resolution 1.80 Å R-free 0.232

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PZI8_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–1003; UniProt 1–1058

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 7cnd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7cnd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7cnd
Deposition date deposition_date2020-07-31
Structure title titleNCI-1 in complex with CRM1-Ran-RanBP1
Keywords keywordsActive Ran, Complex, TRANSPORT PROTEIN, inhibitor; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.18
Radius of gyration Rg (electron density) rg_electron35.36
Forward intensity I(0) i0341939000.00
Molecular weight molecular_weight153920.0 kDa
Excluded volume excluded_volume194450 ų
Envelope volume envelope_volume251540 ų
Hydration-shell volume shell_volume57306 ų
Envelope diameter envelope_diameter108.5
Shell Rg shell_rg43.70
Envelope Rg envelope_rg34.57
Shape Rg shape_rg35.37
Total Rg total_rg35.91
Total atoms total_atoms10809
Residues n_residues1324
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 dmax109.4
Rg (real space) rg_real35.92
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real3.4190e+08
I(0) uncertainty (real space) i0_real_error5.4010e+06
Rg (reciprocal space) rg_reciprocal36.08
I(0) (reciprocal space) i0_reciprocal342000000.0000
Solution quality estimate total_estimate0.9070
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.2
Skewness Skewness skewness0.027
Kurtosis Kurtosis kurtosis-0.620
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha44290000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd7cnda_
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_idd7cndb_
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.0 — automated matches

8. Citations (1)

9. Files and Curves (10)