2k0c

Zinc-finger 2 of Nup153

Method: SOLUTION NMR Dmax: 39.1 Å Quality: REASONABLE

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

Nuclear pore complex protein Nup153

Rattus norvegicus

UniProt P49791

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 703–755 Fragment:RanBP2-type 2 domain (UNP residues 703-755) ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions:pH 7;293 K;Pressure ambient NMR sample composition:0.9-1.2 mM nup153znf2, 0.9-1.2 mM ZINC ION, 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.

12 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU153_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–53; UniProt 703–755

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 2k0c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2k0c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2k0c
Deposition date deposition_date2008-01-31
Structure title titleZinc-finger 2 of Nup153
Keywords keywords;Zinc-Finger, DNA-binding, Metal-binding, mRNA transport, Nuclear pore complex, Nucleus, Phosphoprotein, Protein transport, Translocation, Transport, METAL BINDING PROTEIN ;; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier9.98
Radius of gyration Rg (electron density) rg_electron10.35
Forward intensity I(0) i095438600.00
Molecular weight molecular_weight75714.0 kDa
Excluded volume excluded_volume92591 ų
Envelope volume envelope_volume18622 ų
Hydration-shell volume shell_volume11097 ų
Envelope diameter envelope_diameter44.7
Shell Rg shell_rg20.05
Envelope Rg envelope_rg15.48
Shape Rg shape_rg10.32
Total Rg total_rg10.91
Total atoms total_atoms10280
Residues n_residues700
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 dmax39.1
Rg (real space) rg_real10.15
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real9.5440e+07
I(0) uncertainty (real space) i0_real_error1.0660e+06
Rg (reciprocal space) rg_reciprocal10.15
I(0) (reciprocal space) i0_reciprocal95440000.0000
Solution quality estimate total_estimate0.6857
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary11.4
Skewness Skewness skewness0.679
Kurtosis Kurtosis kurtosis0.303
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12630.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.521; Stabil: 0.988; Sysdev: 1.000; Positv: 1.000; Valcen: 0.382; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2k0ca_
Class classg — Small proteins
Fold Fold foldg.41 — Rubredoxin-like
Superfamily Superfamily superfamilyg.41.11 — Ran binding protein zinc finger-like
Family Family familyg.41.11.1 — Ran binding protein zinc finger-like

8. Citations (1)

9. Files and Curves (10)