8pjn

Catalytic module of human CTLH E3 ligase bound to multiphosphorylated UBE2H~ubiquitin

Method: ELECTRON MICROSCOPY Dmax: 132.0 Å Quality: GOOD

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

E3 ubiquitin-protein transferase RMND5A

Homo sapiens

UniProt Q9H871

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 1–391 Not recorded Ubiquitin-conjugating enzyme E2 H × 1 (P62256) E3 ubiquitin-protein transferase MAEA × 1 (Q7L5Y9) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

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 RMD5A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain b; PDBConstruct 1–391; UniProt 1–391

Ubiquitin-conjugating enzyme E2 H

Homo sapiens

UniProt P62256

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 2; UniProt 1–183 Mutation:C87K Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein transferase RMND5A × 1 (Q9H871) E3 ubiquitin-protein transferase MAEA × 1 (Q7L5Y9) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBE2H_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–183; UniProt 1–183

E3 ubiquitin-protein transferase MAEA

Homo sapiens

UniProt Q7L5Y9

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 i; UniProt 1–396 Not recorded E3 ubiquitin-protein transferase RMND5A × 1 (Q9H871) Ubiquitin-conjugating enzyme E2 H × 1 (P62256) Ubiquitin × 1 (P0CG48) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

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 MAEA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain i; PDBConstruct 1–396; UniProt 1–396

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 u; UniProt 1–76 Not recorded E3 ubiquitin-protein transferase RMND5A × 1 (Q9H871) Ubiquitin-conjugating enzyme E2 H × 1 (P62256) E3 ubiquitin-protein transferase MAEA × 1 (Q7L5Y9) ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

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 u; 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 8pjn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pjn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8pjn
Deposition date deposition_date2023-06-23
Structure title titleCatalytic module of human CTLH E3 ligase bound to multiphosphorylated UBE2H~ubiquitin
Keywords keywordsE3 ubiquitin ligase, E2 ubiquitin-conjugating enzyme, phosphorylation, CTLH, GID, UBE2H, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.29
Radius of gyration Rg (electron density) rg_electron38.57
Forward intensity I(0) i0152000000.00
Molecular weight molecular_weight98802.0 kDa
Excluded volume excluded_volume123630 ų
Envelope volume envelope_volume174530 ų
Hydration-shell volume shell_volume40486 ų
Envelope diameter envelope_diameter136.7
Shell Rg shell_rg41.25
Envelope Rg envelope_rg38.21
Shape Rg shape_rg38.60
Total Rg total_rg38.69
Total atoms total_atoms6917
Residues n_residues916
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 dmax132.0
Rg (real space) rg_real38.57
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real1.5200e+08
I(0) uncertainty (real space) i0_real_error3.2020e+06
Rg (reciprocal space) rg_reciprocal38.40
I(0) (reciprocal space) i0_reciprocal152000000.0000
Solution quality estimate total_estimate0.8541
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.8
Skewness Skewness skewness0.472
Kurtosis Kurtosis kurtosis-0.279
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16330000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.892; Smooth: 0.674

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)