9lky

Dimer of CRL2-FEM1B bound with PLD6

Method: ELECTRON MICROSCOPY Dmax: 194.9 Å Quality: GOOD

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

Mitochondrial cardiolipin hydrolase

Homo sapiens

UniProt Q8N2A8

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain K; UniProt 36–239 Not recorded Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein fem-1 homolog B × 2 (Q9UK73) Elongin-B × 2 (Q15370) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 PLD6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 1–204; UniProt 36–239

Cullin-2

Homo sapiens

UniProt Q13617

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain A; UniProt 2–744 Chain B; UniProt 2–744 Not recorded Mitochondrial cardiolipin hydrolase × 1 (Q8N2A8) Elongin-C × 2 (Q15369) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein fem-1 homolog B × 2 (Q9UK73) Elongin-B × 2 (Q15370) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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.

41 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 22–764; UniProt 2–744 Author chain B; PDBConstruct 22–764; UniProt 2–744

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain C; UniProt 17–112 Chain G; UniProt 17–112 Not recorded Mitochondrial cardiolipin hydrolase × 1 (Q8N2A8) Cullin-2 × 2 (Q13617) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein fem-1 homolog B × 2 (Q9UK73) Elongin-B × 2 (Q15370) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–96; UniProt 17–112 Author chain G; PDBConstruct 1–96; UniProt 17–112

E3 ubiquitin-protein ligase RBX1, N-terminally processed

Homo sapiens

UniProt P62877

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain E; UniProt 16–108 Chain I; UniProt 16–108 Not recorded Mitochondrial cardiolipin hydrolase × 1 (Q8N2A8) Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) Protein fem-1 homolog B × 2 (Q9UK73) Elongin-B × 2 (Q15370) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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.

99 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 4–96; UniProt 16–108 Author chain I; PDBConstruct 4–96; UniProt 16–108

Protein fem-1 homolog B

Homo sapiens

UniProt Q9UK73

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain F; UniProt 1–627 Chain J; UniProt 1–627 Not recorded Mitochondrial cardiolipin hydrolase × 1 (Q8N2A8) Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Elongin-B × 2 (Q15370) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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.

30 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FEM1B_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–627; UniProt 1–627 Author chain J; PDBConstruct 1–627; UniProt 1–627

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain D; UniProt 1–118 Chain H; UniProt 1–118 Not recorded Mitochondrial cardiolipin hydrolase × 1 (Q8N2A8) Cullin-2 × 2 (Q13617) Elongin-C × 2 (Q15369) E3 ubiquitin-protein ligase RBX1, N-terminally processed × 2 (P62877) Protein fem-1 homolog B × 2 (Q9UK73) ZN ZINC ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 6
Chains and sequence ranges Author chain D; PDBConstruct 1–118; UniProt 1–118 Author chain H; PDBConstruct 1–118; UniProt 1–118

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 9lky

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9lky
Deposition date deposition_date2025-01-17
Structure title titleDimer of CRL2-FEM1B bound with PLD6
Keywords keywordsubiquitination E3 ligase, Cryo-EM, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.66
Radius of gyration Rg (electron density) rg_electron60.47
Forward intensity I(0) i02011360000.00
Molecular weight molecular_weight375070.0 kDa
Excluded volume excluded_volume468780 ų
Envelope volume envelope_volume761960 ų
Hydration-shell volume shell_volume106000 ų
Envelope diameter envelope_diameter196.1
Shell Rg shell_rg62.73
Envelope Rg envelope_rg57.77
Shape Rg shape_rg60.49
Total Rg total_rg60.45
Total atoms total_atoms26308
Residues n_residues3277
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 dmax194.9
Rg (real space) rg_real60.47
Rg uncertainty (real space) rg_real_error1.99
I(0) (real space) i0_real2.0110e+09
I(0) uncertainty (real space) i0_real_error4.6100e+07
Rg (reciprocal space) rg_reciprocal60.80
I(0) (reciprocal space) i0_reciprocal2012000000.0000
Solution quality estimate total_estimate0.8615
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.0
Skewness Skewness skewness0.166
Kurtosis Kurtosis kurtosis-0.463
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha72110000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.434

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)