2lgv

Rbx1

Method: SOLUTION NMR Dmax: 40.9 Å Quality: REASONABLE

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

E3 ubiquitin-protein ligase RBX1

Homo sapiens

UniProt P62877

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 12–108 Fragment:sequence database residues 12-108 Mutation:W27S, V30S, L32Q, W33S ZN ZINC ION × 3 SOLUTION NMR NMR measurement conditions:pH 7.5;298 K;Ionic strength (raw mmCIF value) 0.120;Pressure ambient NMR sample composition:20 mM sodium phosphate, 100 mM sodium chloride, 1 mM DTT, 700 uM [U-98% 15N] protein, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:20 mM sodium phosphate, 100 mM sodium chloride, 1 mM DTT, 700 uM [U-98% 13C; U-98% 15N] protein, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:20 mM sodium phosphate, 100 mM sodium chloride, 1 mM DTT, 700 uM [U-98% 13C; U-98% 15N] protein, 100% D2O | 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.

99 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–100; UniProt 12–108

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 2lgv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2lgv
Deposition date deposition_date2011-08-02
Structure title titleRbx1
Keywords keywordsROC1, RING, Zn-binding, LIGASE; LIGASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.56
Radius of gyration Rg (electron density) rg_electron15.64
Forward intensity I(0) i0908133000.00
Molecular weight molecular_weight227130.0 kDa
Excluded volume excluded_volume272690 ų
Envelope volume envelope_volume79226 ų
Hydration-shell volume shell_volume26274 ų
Envelope diameter envelope_diameter118.8
Shell Rg shell_rg31.77
Envelope Rg envelope_rg29.25
Shape Rg shape_rg15.70
Total Rg total_rg15.96
Total atoms total_atoms30140
Residues n_residues2000
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 dmax40.9
Rg (real space) rg_real13.76
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real8.5220e+08
I(0) uncertainty (real space) i0_real_error7.8050e+06
Rg (reciprocal space) rg_reciprocal16.14
I(0) (reciprocal space) i0_reciprocal908100000.0000
Solution quality estimate total_estimate0.6784
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.0
Skewness Skewness skewness0.363
Kurtosis Kurtosis kurtosis-0.220
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.0050
Highest regularization parameter α highest_alpha343200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.074; Oscil: 0.956; Stabil: 0.986; Sysdev: 0.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2lgva1
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.1 — RING finger domain, C3HC4
Domain ID domain_idd2lgva2
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_id2lgvA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)

8. Citations (1)

9. Files and Curves (10)