← Back to search
7qpb

Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle

Method: X-RAY DIFFRACTION
▼

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

Isoform I of Ubiquitin-protein ligase E3A

Homo sapiens

UniProt Q05086

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 hybrid foldamer-peptide macrocycle × 1 water × 3 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 6 hybrid foldamer-peptide macrocycle × 2 water × 6 Consistent with protein count
3 Protein heterocomplex Heteromer Protein 3 hybrid foldamer-peptide macrocycle × 1 water × 2 Consistent with protein count
4 Protein heterocomplex Heteromer Protein 6 hybrid foldamer-peptide macrocycle × 2 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1eqx 8enp 8ept 9vg5

4 assemblies

Homodimer
6tgk

1 assemblies

Homotetramer

None

Other homooligomers
1d5f

1 assemblies

Heteromeric or nucleic-acid complex
1c4z 4giz 4giz 6sjv 6slm 6u19 7qpb 7qpb 7qpb 7qpb 8gcr 8jrn

20 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name UBE3A_HUMAN
Isoform Q05086-2
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–114； UniProt 741–852 Author chain B； PDBConstruct 3–114； UniProt 741–852 Author chain C； PDBConstruct 3–114； UniProt 741–852 Author chain D； PDBConstruct 3–114； UniProt 741–852

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id7qpb
Deposition date deposition_date2022-01-03
Structure title titleCatalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle
Keywords keywordsHect, E3 ligase catalytic domain, ubiquitin protein ligase, transferase activity, catalytic activity, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION
▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

7qpb__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

7qpb__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

7qpb__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）20.76 Å
Rg (electron density)19.87 Å
Total Rg20.73 Å
Atom count1855
Residues221
Excluded volume33118 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7qpb__assembly_1__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 7qpb__assembly_2__model_1 hexameric （6） Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 7qpb__assembly_3__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 7qpb__assembly_4__model_1 hexameric （6） Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (3)

▶

7. Citations (1)