9lk2

monomeric ZYG11B-EloB-EloC + substrate peptide GYIND

Method: ELECTRON MICROSCOPY Dmax: 120.6 Å Quality: GOOD

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

Protein zyg-11 homolog B,Green fluorescent protein

Homo sapiens

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–238 Mutation:F821L/S822T/Q837R/F856S/M910T/V920A Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) GLY-TYR-ILE-ASN-ASP × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 759–995; UniProt 2–238

Protein zyg-11 homolog B,Green fluorescent protein

Homo sapiens

UniProt Q9C0D3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–744 Mutation:F821L/S822T/Q837R/F856S/M910T/V920A Elongin-B × 1 (Q15370) Elongin-C × 1 (Q15369) GLY-TYR-ILE-ASN-ASP × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ZY11B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–744; UniProt 1–744

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 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–118 Not recorded Protein zyg-11 homolog B,Green fluorescent protein × 1 (Q9C0D3,P42212) Elongin-C × 1 (Q15369) GLY-TYR-ILE-ASN-ASP × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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 2
Chains and sequence ranges Author chain B; PDBConstruct 20–137; 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 Insufficient information Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–112 Not recorded Protein zyg-11 homolog B,Green fluorescent protein × 1 (Q9C0D3,P42212) Elongin-B × 1 (Q15370) GLY-TYR-ILE-ASN-ASP × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.37 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 1–112; UniProt 1–112

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 9lk2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9lk2
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9lk2
Deposition date deposition_date2025-01-15
Structure title titlemonomeric ZYG11B-EloB-EloC + substrate peptide GYIND
Keywords keywordsmonomeric ZYG11B-EloB-EloC with substrate peptide GYIND, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.50
Radius of gyration Rg (electron density) rg_electron35.94
Forward intensity I(0) i0156062000.00
Molecular weight molecular_weight101370.0 kDa
Excluded volume excluded_volume127440 ų
Envelope volume envelope_volume175790 ų
Hydration-shell volume shell_volume41732 ų
Envelope diameter envelope_diameter120.2
Shell Rg shell_rg41.43
Envelope Rg envelope_rg35.21
Shape Rg shape_rg35.96
Total Rg total_rg36.25
Total atoms total_atoms7117
Residues n_residues900
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 dmax120.6
Rg (real space) rg_real36.48
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real1.5610e+08
I(0) uncertainty (real space) i0_real_error2.2380e+06
Rg (reciprocal space) rg_reciprocal36.50
I(0) (reciprocal space) i0_reciprocal156100000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26360000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)