7rma

Structure of the fourth UIM (Ubiquitin Interacting Motif) of ANKRD13D in complex with a high affinity UbV (Ubiquitin Variant)

Method: X-RAY DIFFRACTION Dmax: 59.3 Å Quality: GOOD

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

Ubiquitin Variant

Homo sapiens

UniProt P0CG47

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–79 Not recorded Ankyrin repeat domain-containing protein 13D × 2 (Q6ZTN6) SO4 SULFATE ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;298 K;0.1M Li2SO4, 0.1M sodium acetate pH 4.5 and 50% PEG 400. Crystals were cryoprotected in this buffer plus 20% ethylene glycol Resolution 2.00 Å R-free 0.246

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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–85; UniProt 1–79

Ankyrin repeat domain-containing protein 13D

OrganismNot specified

UniProt Q6ZTN6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 499–518 Not recorded Ubiquitin Variant × 2 (P0CG47) SO4 SULFATE ION × 2 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;298 K;0.1M Li2SO4, 0.1M sodium acetate pH 4.5 and 50% PEG 400. Crystals were cryoprotected in this buffer plus 20% ethylene glycol Resolution 2.00 Å R-free 0.246

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name AN13D_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 499–518

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 7rma

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7rma
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7rma
Deposition date deposition_date2021-07-27
Structure title titleStructure of the fourth UIM (Ubiquitin Interacting Motif) of ANKRD13D in complex with a high affinity UbV (Ubiquitin Variant)
Keywords keywords;Ubiquitin-interacting motif, UIM, Ubiquitin Variant, protein engineering, protein recognition, strand-exchange dimer, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.58
Radius of gyration Rg (electron density) rg_electron14.44
Forward intensity I(0) i02514150.00
Molecular weight molecular_weight10692.0 kDa
Excluded volume excluded_volume13338 ų
Envelope volume envelope_volume17106 ų
Hydration-shell volume shell_volume10765 ų
Envelope diameter envelope_diameter57.0
Shell Rg shell_rg19.31
Envelope Rg envelope_rg15.25
Shape Rg shape_rg14.37
Total Rg total_rg15.75
Total atoms total_atoms752
Residues n_residues94
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 dmax59.3
Rg (real space) rg_real15.65
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real2.5140e+06
I(0) uncertainty (real space) i0_real_error3.2830e+04
Rg (reciprocal space) rg_reciprocal15.64
I(0) (reciprocal space) i0_reciprocal2514000.0000
Solution quality estimate total_estimate0.7735
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.5
Skewness Skewness skewness0.619
Kurtosis Kurtosis kurtosis0.733
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha430600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.398; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.868; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)