7R70: UbArk2C fusion protein

Crystal Structure of the UbArk2C fusion protein. Determined by X-ray diffraction at 2.5 Å resolution. Released 9 Mar 2022.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,436
Mol. weight: 41.3 kDa
Ligands: ZN
Released: 9 Mar 2022

Explore 7R70 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7R70 contains 16 α-helices and 28 β-strands across 2 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, 14 β-strands

Element	Residues	Length	Sheet
β-strand	1-6	6	1
β-strand	12-17	6	1
β-strand	22	1	2
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	1
β-strand	48-49	2	1
β-strand	55	1	2
α-helix	56-58	3
β-strand	66-71	6	1
α-helix	258-264	7
β-strand	266-269	4	3
β-strand	293	1	4
α-helix	299	1
β-strand	300	1	4
α-helix	301	1
β-strand	306-309	4	3
β-strand	315-317	3	3
α-helix	318-327	10
β-strand	330	1	5
β-strand	337	1	5

Chain B: 9 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	1-6	6	6
β-strand	12-17	6	6
β-strand	22	1	7
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	6
β-strand	48-49	2	6
α-helix	50-51	2
β-strand	55	1	7
α-helix	57-59	3
β-strand	66-71	6	6
α-helix	261-264	4
β-strand	266-269	4	8
α-helix	272-274	3
β-strand	293	1	9
α-helix	299	1
β-strand	300	1	9
α-helix	301	1
β-strand	306-309	4	8
β-strand	315-317	3	8
α-helix	318-328	11
β-strand	330	1	10
β-strand	337	1	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin,E3 ubiquitin-protein ligase RNF165	A, B	protein	183	Homo sapiens	P0CG48 (AlphaFold model), Q6ZSG1 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7R70_1 Ubiquitin,E3 ubiquitin-protein ligase RNF165 (chains A, B)
GPLGSMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRT
LSDYNIQKESTLHLVLRLRGGGESGSGGSGSGAVQNTIERFTFPHKYKKRRPQDGKGKKD
EGEESDTDEKCTICLSMLEDGEDVRRLPCMHLFHQLCVDQWLAMSKKCPICRVDIETQLG
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Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	4

Water and common crystallization additives (GOL) are not listed.

Primary citation

Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C. Paluda, A., Middleton, A.J., Rossig, C. et al. Nat Commun (2022) 13:1181-1181. DOI 10.1038/s41467-022-28782-y · PubMed

Other PDB entries of the same protein (UniProt P0CG48 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6Q00 0.85 Å, TDP2 UBA Domain Bound to Ubiquitin at 0.85 Angstroms Resolution, Crystal Form 1
1OGW 1.32 Å, Synthetic Ubiquitin with fluoro-Leu at 50 and 67
5NL4 1.32 Å, Crystal structure of Zn1.3-E16V human ubiquitin (hUb) mutant adduct, from a solution 35…
2GBJ 1.35 Å, Crystal Structure of the 9-10 8 Glycine Insertion Mutant of Ubiquitin.
4HK2 1.4 Å, U7Ub25.2540
9FJ3 1.4 Å, Structure of ubiquitin bound of coiled-coil UIM form 2
1XD3 1.45 Å, Crystal structure of UCHL3-UbVME complex
4IUM 1.45 Å, Equine arteritis virus papain-like protease 2 (PLP2) covalently bound to ubiquitin
7UV5 1.45 Å, The crystal structure of Papain-Like Protease of SARS CoV-2, C111S/D286N mutant, in…
5NLF 1.5 Å, Crystal structure of Zn2.7-E16V human ubiquitin (hUb) mutant adduct, from a solution 100…
9F6G 1.5 Å, Human USP30 chimera bound to Ubiquitin-PA
9OVX 1.5 Å, Crystal structure of ubiquitin K27M mutant

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