9oma

Cryo-EM structure of PCMTD1-ELOBC-CUL5-RBX2 (CRL5-PCMTD1)

Method: ELECTRON MICROSCOPY Dmax: 173.6 Å Quality: GOOD

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

Protein-L-isoaspartate O-methyltransferase domain-containing protein 1

Homo sapiens

UniProt Q96MG8

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–357 Mutation:N312I Cullin-5 × 1 (Q93034) RING-box protein 2 × 1 (Q9UBF6) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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 PCMD1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–358; UniProt 1–357

Cullin-5

Homo sapiens

UniProt Q93034

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–780 Not recorded Protein-L-isoaspartate O-methyltransferase domain-containing protein 1 × 1 (Q96MG8) RING-box protein 2 × 1 (Q9UBF6) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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.

13 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–783; UniProt 1–780

RING-box protein 2

Homo sapiens

UniProt Q9UBF6

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–113 Not recorded Protein-L-isoaspartate O-methyltransferase domain-containing protein 1 × 1 (Q96MG8) Cullin-5 × 1 (Q93034) Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–113; UniProt 1–113

Elongin-B

Homo sapiens

UniProt Q15370

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1–118 Not recorded Protein-L-isoaspartate O-methyltransferase domain-containing protein 1 × 1 (Q96MG8) Cullin-5 × 1 (Q93034) RING-box protein 2 × 1 (Q9UBF6) Elongin-C × 1 (Q15369) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–118; UniProt 1–118

Elongin-C

Homo sapiens

UniProt Q15369

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 17–112 Not recorded Protein-L-isoaspartate O-methyltransferase domain-containing protein 1 × 1 (Q96MG8) Cullin-5 × 1 (Q93034) RING-box protein 2 × 1 (Q9UBF6) Elongin-B × 1 (Q15370) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.14 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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–96; UniProt 17–112

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 9oma

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9oma
Deposition date deposition_date2025-05-13
Structure title titleCryo-EM structure of PCMTD1-ELOBC-CUL5-RBX2 (CRL5-PCMTD1)
Keywords keywordsCUL5-RING ubiquitin ligase complex, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.59
Radius of gyration Rg (electron density) rg_electron59.01
Forward intensity I(0) i0300010000.00
Molecular weight molecular_weight147050.0 kDa
Excluded volume excluded_volume184960 ų
Envelope volume envelope_volume319190 ų
Hydration-shell volume shell_volume46018 ų
Envelope diameter envelope_diameter182.3
Shell Rg shell_rg61.70
Envelope Rg envelope_rg55.14
Shape Rg shape_rg59.04
Total Rg total_rg58.98
Total atoms total_atoms10325
Residues n_residues1270
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 dmax173.6
Rg (real space) rg_real59.02
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real3.0000e+08
I(0) uncertainty (real space) i0_real_error6.2470e+06
Rg (reciprocal space) rg_reciprocal58.16
I(0) (reciprocal space) i0_reciprocal299600000.0000
Solution quality estimate total_estimate0.7660
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-1.012
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8979000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.563; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)