5bxq

Structure of the NTF2:RanGDP complex

Method: X-RAY DIFFRACTION Dmax: 115.7 Å Quality: GOOD

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

Nuclear transport factor 2

Rattus norvegicus

UniProt P61972

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–127 Chain B; UniProt 1–127 Not recorded GTP-binding nuclear protein Ran × 3 (P62825) GDP GUANOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M Li2SO4, 50 mM Na Citrate pH5.6, 15% PEG4000 Resolution 2.50 Å R-free 0.225

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NTF2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–127; UniProt 1–127 Author chain B; PDBConstruct 1–127; UniProt 1–127

GTP-binding nuclear protein Ran

Canis familiaris

UniProt P62825

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–216 Chain D; UniProt 1–216 Chain E; UniProt 1–216 Not recorded Nuclear transport factor 2 × 2 (P61972) GDP GUANOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1 M Li2SO4, 50 mM Na Citrate pH5.6, 15% PEG4000 Resolution 2.50 Å R-free 0.225

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 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAN_CANFA
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–216; UniProt 1–216 Author chain D; PDBConstruct 1–216; UniProt 1–216 Author chain E; PDBConstruct 1–216; 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 5bxq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5bxq
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5bxq
Deposition date deposition_date2015-06-09
Structure title titleStructure of the NTF2:RanGDP complex
Keywords keywordsNuclear transport, RanGDP, NTF2, transport protein; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.19
Radius of gyration Rg (electron density) rg_electron36.08
Forward intensity I(0) i0140025000.00
Molecular weight molecular_weight96858.0 kDa
Excluded volume excluded_volume121770 ų
Envelope volume envelope_volume158000 ų
Hydration-shell volume shell_volume38589 ų
Envelope diameter envelope_diameter120.9
Shell Rg shell_rg40.12
Envelope Rg envelope_rg35.88
Shape Rg shape_rg36.07
Total Rg total_rg36.38
Total atoms total_atoms6824
Residues n_residues841
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 dmax115.7
Rg (real space) rg_real36.25
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real1.4000e+08
I(0) uncertainty (real space) i0_real_error2.2700e+06
Rg (reciprocal space) rg_reciprocal36.22
I(0) (reciprocal space) i0_reciprocal140000000.0000
Solution quality estimate total_estimate0.8786
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.678
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46990000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.902; Smooth: 0.749

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd5bxqa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.4 — NTF2-like
Family Family familyd.17.4.2 — NTF2-like
Domain ID domain_idd5bxqb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.17 — Cystatin-like
Superfamily Superfamily superfamilyd.17.4 — NTF2-like
Family Family familyd.17.4.2 — NTF2-like
Domain ID domain_idd5bxqc_
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_idd5bxqd_
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_idd5bxqe_
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 (5 domains)

Domain ID domain_id5bxqA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily50
Domain ID domain_id5bxqB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily50
Domain ID domain_id5bxqC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5bxqD00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5bxqE00
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)