9n1f

Crystal Structure of the Ark2C-Ubc13~Ub-Mms2 complex

Method: X-RAY DIFFRACTION Dmax: 88.7 Å Quality: EXCELLENT

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

E3 ubiquitin-protein ligase ARK2C

Homo sapiens

UniProt Q6ZSG1

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 255–346 Not recorded Ubiquitin-conjugating enzyme E2 N × 1 (P61088) Ubiquitin-conjugating enzyme E2 variant 2 × 1 (Q15819) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M Sodium Malonate and 18% w/v PEG 3350 Resolution 2.10 Å R-free 0.279

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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARK2C_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–87; UniProt 255–346

Ubiquitin-conjugating enzyme E2 N

Homo sapiens

UniProt P61088

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 B; UniProt 1–152 Mutation:C87K, K92T, K94Q E3 ubiquitin-protein ligase ARK2C × 1 (Q6ZSG1) Ubiquitin-conjugating enzyme E2 variant 2 × 1 (Q15819) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M Sodium Malonate and 18% w/v PEG 3350 Resolution 2.10 Å R-free 0.279

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.

43 other PDB entries and 73 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBE2N_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–157; UniProt 1–152

Ubiquitin-conjugating enzyme E2 variant 2

Homo sapiens

UniProt Q15819

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 1–145 Mutation:S32A E3 ubiquitin-protein ligase ARK2C × 1 (Q6ZSG1) Ubiquitin-conjugating enzyme E2 N × 1 (P61088) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M Sodium Malonate and 18% w/v PEG 3350 Resolution 2.10 Å R-free 0.279

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.

17 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2V2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–145; UniProt 1–145

Ubiquitin

Homo sapiens

UniProt P0CG48

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 D; UniProt 1–76 Not recorded E3 ubiquitin-protein ligase ARK2C × 1 (Q6ZSG1) Ubiquitin-conjugating enzyme E2 N × 1 (P61088) Ubiquitin-conjugating enzyme E2 variant 2 × 1 (Q15819) ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289.15 K;0.1 M Sodium Malonate and 18% w/v PEG 3350 Resolution 2.10 Å R-free 0.279

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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–76; UniProt 1–76

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 9n1f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n1f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n1f
Deposition date deposition_date2025-01-26
Structure title titleCrystal Structure of the Ark2C-Ubc13~Ub-Mms2 complex
Keywords keywordsRING E3 ligase Ubiquitin PTM, LIGASE, E2~Ub conjugate, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.01
Radius of gyration Rg (electron density) rg_electron27.97
Forward intensity I(0) i040661400.00
Molecular weight molecular_weight49548.0 kDa
Excluded volume excluded_volume62091 ų
Envelope volume envelope_volume82276 ų
Hydration-shell volume shell_volume25461 ų
Envelope diameter envelope_diameter91.0
Shell Rg shell_rg33.98
Envelope Rg envelope_rg27.68
Shape Rg shape_rg27.94
Total Rg total_rg28.71
Total atoms total_atoms3471
Residues n_residues434
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 dmax88.7
Rg (real space) rg_real28.91
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real4.0660e+07
I(0) uncertainty (real space) i0_real_error5.7330e+05
Rg (reciprocal space) rg_reciprocal28.96
I(0) (reciprocal space) i0_reciprocal40660000.0000
Solution quality estimate total_estimate0.9079
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.6
Skewness Skewness skewness0.059
Kurtosis Kurtosis kurtosis-0.759
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6078000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)