2vok

Murine TRIM21

Method: X-RAY DIFFRACTION Dmax: 80.4 Å Quality: GOOD

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

52 KDA RO PROTEIN

MUS MUSCULUS

UniProt Q62191

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 291–470 Chain B; UniProt 291–470 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.30 Å R-free 0.236

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.

112 other PDB entries and 112 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RO52_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–188; UniProt 291–470 Author chain B; PDBConstruct 9–188; UniProt 291–470

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 2vok

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2vok
Deposition date deposition_date2008-02-19
Structure title titleMurine TRIM21
Keywords keywords;POLYMORPHISM, IMMUNE SYSTEM, METAL-BINDING, TRIPARTITE MOTIF (TRIM) PROTEIN, SPRY SYSTEMIC LUPUS ERYTHEMATOSUS, ZINC, B30.2, RO.52, NUCLEUS, PRYSPRY, CYTOPLASM, RIBONUCLEOPROTEIN, SYSTEMIC LUPUS ERYTHEMATOSUS, ZINC-FINGER, DNA-BINDING, RNA-BINDING, COILED COIL ;; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.46
Radius of gyration Rg (electron density) rg_electron22.64
Forward intensity I(0) i031450600.00
Molecular weight molecular_weight42361.0 kDa
Excluded volume excluded_volume52586 ų
Envelope volume envelope_volume61817 ų
Hydration-shell volume shell_volume23498 ų
Envelope diameter envelope_diameter82.5
Shell Rg shell_rg28.94
Envelope Rg envelope_rg22.61
Shape Rg shape_rg22.62
Total Rg total_rg23.44
Total atoms total_atoms2995
Residues n_residues371
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 dmax80.4
Rg (real space) rg_real23.50
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real3.1450e+07
I(0) uncertainty (real space) i0_real_error3.6910e+05
Rg (reciprocal space) rg_reciprocal23.49
I(0) (reciprocal space) i0_reciprocal31450000.0000
Solution quality estimate total_estimate0.8602
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.0
Skewness Skewness skewness0.439
Kurtosis Kurtosis kurtosis-0.255
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8021000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.748; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.963; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2voka1
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.22 — SPRY domain
Domain ID domain_idd2voka2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2vokb1
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.22 — SPRY domain
Domain ID domain_idd2vokb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id2vokA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily920 — SPRY domain
Domain ID domain_id2vokB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily920 — SPRY domain

8. Citations (1)

9. Files and Curves (10)