1rrp

STRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX

Method: X-RAY DIFFRACTION Dmax: 109.2 Å Quality: GOOD

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

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 8–211 Not recorded NUCLEAR PORE COMPLEX PROTEIN NUP358 × 1 (P49792) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.25;pH 6.25 Resolution 2.96 Å R-free 0.304
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 8–211 Not recorded NUCLEAR PORE COMPLEX PROTEIN NUP358 × 1 (P49792) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.25;pH 6.25 Resolution 2.96 Å R-free 0.304
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 8–211 Chain C; UniProt 8–211 Not recorded NUCLEAR PORE COMPLEX PROTEIN NUP358 × 4 (P49792) MG MAGNESIUM ION × 4 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.25;pH 6.25 Resolution 2.96 Å R-free 0.304
4 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 8–211 Chain C; UniProt 8–211 Not recorded NUCLEAR PORE COMPLEX PROTEIN NUP358 × 2 (P49792) MG MAGNESIUM ION × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.25;pH 6.25 Resolution 2.96 Å R-free 0.304

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 200 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 1–204; UniProt 8–211 Author chain C; PDBConstruct 1–204; UniProt 8–211

NUCLEAR PORE COMPLEX PROTEIN NUP358

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1171–1304 Not recorded RAN × 1 (P62826) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.25;pH 6.25 Resolution 2.96 Å R-free 0.304
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1171–1304 Not recorded RAN × 1 (P62826) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.25;pH 6.25 Resolution 2.96 Å R-free 0.304
3 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1171–1304 Chain D; UniProt 1171–1304 Not recorded RAN × 4 (P62826) MG MAGNESIUM ION × 4 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.25;pH 6.25 Resolution 2.96 Å R-free 0.304
4 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1171–1304 Chain D; UniProt 1171–1304 Not recorded RAN × 2 (P62826) MG MAGNESIUM ION × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.25;pH 6.25 Resolution 2.96 Å R-free 0.304

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 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBP2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–134; UniProt 1171–1304 Author chain D; PDBConstruct 1–134; UniProt 1171–1304

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 1rrp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1rrp
Deposition date deposition_date1999-01-15
Structure title titleSTRUCTURE OF THE RAN-GPPNHP-RANBD1 COMPLEX
Keywords keywordsCOMPLEX (SMALL GTPASE-NUCLEAR PROTEIN), SMALL GTPASE, NUCLEAR TRANSPORT, COMPLEX (SMALL GTPASE-NUCLEAR PROTEIN) complex; COMPLEX (SMALL GTPASE/NUCLEAR PROTEIN)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.86
Radius of gyration Rg (electron density) rg_electron32.57
Forward intensity I(0) i088933000.00
Molecular weight molecular_weight76162.0 kDa
Excluded volume excluded_volume95903 ų
Envelope volume envelope_volume123330 ų
Hydration-shell volume shell_volume32459 ų
Envelope diameter envelope_diameter108.6
Shell Rg shell_rg38.13
Envelope Rg envelope_rg32.19
Shape Rg shape_rg32.56
Total Rg total_rg33.06
Total atoms total_atoms5366
Residues n_residues652
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 dmax109.2
Rg (real space) rg_real32.99
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real8.8930e+07
I(0) uncertainty (real space) i0_real_error1.4280e+06
Rg (reciprocal space) rg_reciprocal32.94
I(0) (reciprocal space) i0_reciprocal88930000.0000
Solution quality estimate total_estimate0.8761
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.555
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha17830000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.856; Smooth: 0.845

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1rrpa_
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_idd1rrpb_
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_idd1rrpc_
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_idd1rrpd_
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

CATH v4.4 (4 domains)

Domain ID domain_id1rrpA00
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_id1rrpB00
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)
Domain ID domain_id1rrpC00
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_id1rrpD00
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 (7)

9. Files and Curves (10)