2ct7

Solution Structure of the IBR domain of the RING finger protein 31 protein

Method: SOLUTION NMR Dmax: 51.4 Å Quality: REASONABLE

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

RING finger protein 31

Homo sapiens

UniProt Q96EP0

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 779–851 Fragment:IBR domain ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 220;Pressure ambient NMR sample composition:1.55mM IBR domain U-13C,15N; 20mM d-Tris-HCl; 200mM NaCl; 1mM d-DTT; 0.02% NaN3; 0.01mM ZnCl2; 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.

35 other PDB entries and 74 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNF31_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–80; UniProt 779–851

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 2ct7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ct7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ct7
Deposition date deposition_date2005-05-23
Structure title titleSolution Structure of the IBR domain of the RING finger protein 31 protein
Keywords keywords;RING finger protein 31, IBR, structural genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, 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_guinier19.07
Radius of gyration Rg (electron density) rg_electron19.04
Forward intensity I(0) i0704525000.00
Molecular weight molecular_weight201080.0 kDa
Excluded volume excluded_volume242310 ų
Envelope volume envelope_volume91926 ų
Hydration-shell volume shell_volume27680 ų
Envelope diameter envelope_diameter103.4
Shell Rg shell_rg34.40
Envelope Rg envelope_rg30.16
Shape Rg shape_rg19.09
Total Rg total_rg19.41
Total atoms total_atoms26780
Residues n_residues1720
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 dmax51.4
Rg (real space) rg_real17.35
Rg uncertainty (real space) rg_real_error0.12
I(0) (real space) i0_real6.6850e+08
I(0) uncertainty (real space) i0_real_error7.5020e+06
Rg (reciprocal space) rg_reciprocal19.60
I(0) (reciprocal space) i0_reciprocal704500000.0000
Solution quality estimate total_estimate0.6602
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.461
Kurtosis Kurtosis kurtosis-0.504
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha2.5690
Highest regularization parameter α highest_alpha185700.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.966; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 0.754; 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 (3 domains)

Domain ID domain_idd2ct7a1
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.4 — IBR domain
Domain ID domain_idd2ct7a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2ct7a3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)