7QPB: Isoform I of Ubiquitin-protein ligase E3A

Name: PDB 7QPB: Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle
Published: 2023-09-27
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle. Determined by X-ray diffraction at 2.34 Å resolution. Released 27 Sept 2023.

Method: X-ray diffraction
Resolution: 2.34 Å
Organisms: Homo sapiens, synthetic construct
Chains: 6
Atoms: 3,753
Mol. weight: 56.11 kDa
Released: 27 Sept 2023

Explore 7QPB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7QPB contains 32 α-helices and 16 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 7 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	744-750	7
β-strand	752-754	3	1
α-helix	762-772	11
α-helix	776-787	12
α-helix	792-793	2
α-helix	797-800	4
β-strand	803-806	4	1
α-helix	814-815	2
β-strand	816-818	3	1
β-strand	823-826	4	1
α-helix	832-844	13

Chain B: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	744-750	7
β-strand	752-754	3	2
α-helix	762-772	11
α-helix	776-787	12
α-helix	792-793	2
α-helix	797-800	4
β-strand	803-806	4	2
α-helix	814-815	2
β-strand	816-818	3	2
α-helix	819-821	3
β-strand	823-826	4	2
α-helix	832-845	14

Chain C: 8 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	744-750	7
β-strand	752-754	3	3
α-helix	762-772	11
α-helix	776-787	12
α-helix	792-793	2
α-helix	797-800	4
β-strand	803-805	3	3
α-helix	814-815	2
β-strand	816-818	3	3
α-helix	819-821	3
β-strand	823-825	3	3
α-helix	832-843	12

Chain D: 7 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	744-749	6
β-strand	752-754	3	4
α-helix	762-772	11
α-helix	776-786	11
α-helix	797-800	4
β-strand	803-805	3	4
α-helix	814-815	2
β-strand	816-818	3	4
α-helix	819-821	3
β-strand	823-825	3	4
α-helix	832-843	12

Chains H and I: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	8-13	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Isoform I of Ubiquitin-protein ligase E3A	A, B, C, D	protein	114	Homo sapiens	Q05086 (AlphaFold model)
hybrid foldamer-peptide macrocycle	H, I	protein	15	synthetic construct

Sequence of entity 1 (A, B, C, D), FASTA

>7QPB_1 Isoform I of Ubiquitin-protein ligase E3A (chains A, B, C, D)
GPNLDFQALEETTEYDGGYTRDSVLIREFWEIVHSFTDEQKRLFLQFTTGTDRAPVGGLG
KLKMIIAKNGPDTERLPTSHTCFNVLLLPEYSSKEKLKERLLKAITYAKGFGML

Sequence of entity 2 (H, I), FASTA

>7QPB_2 hybrid foldamer-peptide macrocycle (chains H, I)
XXXXGFWRYVYQKCX

Primary citation

Display Selection of a Hybrid Foldamer-Peptide Macrocycle. Dengler, S., Howard, R.T., Morozov, V. et al. Angew Chem Int Ed Engl (2023) 62:e202308408-e202308408. DOI 10.1002/anie.202308408 · PubMed

Other PDB entries of the same protein (UniProt Q05086 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6TGK 1.3 Å, Domain swapped E6AP C-lobe dimer
6SJV 2.03 Å, Structure of HPV18 E6 oncoprotein in complex with mutant E6AP LxxLL motif
4XR8 2.25 Å, Crystal structure of the HPV16 E6/E6AP/p53 ternary complex at 2.25 A resolution
4GIZ 2.55 Å, Crystal structure of full-length human papillomavirus oncoprotein E6 in complex with…
9L3L 2.59 Å, Crystal structure of the C lobe of E6AP in complex with K48-linked diUb
1C4Z 2.6 Å, Structure of an E6AP-UBCH7 complex: insights into the ubiquitination pathway
8JRN 2.6 Å, Structure of E6AP-E6 complex in Att1 state
1D5F 2.8 Å, Structure of E6AP: insights into ubiquitination pathway
6SLM 2.8 Å, Crystal structure of full-length HPV31 E6 oncoprotein in complex with LXXLL peptide of…
8JRO 3.01 Å, Structure of E6AP-E6 complex in Att2 state
7Q41 3.01 Å, Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with…
9U4A 3.3 Å, Structure of UBE3A T485E tetramer

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