3K9O: E2-25K and UBB+1 complex

The crystal structure of E2-25K and UBB+1 complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 8 Sept 2010.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,326
Mol. weight: 33.31 kDa
Released: 8 Sept 2010

Explore 3K9O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3K9O contains 17 α-helices and 15 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: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	6-17	12
α-helix	20-23	4
β-strand	27-31	5	1
β-strand	38-44	7	1
α-helix	45-46	2
β-strand	55-61	7	1
α-helix	70-71	2
β-strand	72-75	4	1
β-strand	81	1	2
β-strand	84	1	2
β-strand	90	1	1
β-strand	91	1	2
α-helix	94-96	3
α-helix	106-118	13
α-helix	128-136	9
α-helix	138-153	16
α-helix	155-157	3
α-helix	160-170	11
α-helix	176-185	10
α-helix	190-199	10

Chain B: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	3
β-strand	12-16	5	3
β-strand	22	1	4
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	3
β-strand	48-49	2	3
α-helix	50-51	2
β-strand	55	1	4
α-helix	57-59	3
β-strand	66-71	6	3
α-helix	72-73	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 K	A	protein	201	Homo sapiens	P61086 (AlphaFold model)
Ubiquitin	B	protein	96	Homo sapiens	P0CG48 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3K9O_1 Ubiquitin-conjugating enzyme E2 K (chains A)
GMANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLE
IKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAA
AEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAV
IVALSSKSWDVETATELLLSN

Sequence of entity 2 (B), FASTA

>3K9O_2 Ubiquitin (chains B)
GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDY
NIQKESTLHLVLRLRGYADLREDPDRQDHHPGSGAQ

Primary citation

Structural Basis of E2-25K/UBB+1 Interaction for Neurotoxicity of Alzheimer Disease by Proteasome Inhibition. Kang, G.B., Ko, S., Song, S.M. et al. To be published.

Other PDB entries of the same protein (UniProt P61086 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3E46 1.86 Å, Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington interacting…
5DFL 2.1 Å, Crystal structure of Ube2K~Ubiquitin conjugate
6JB7 2.1 Å, Crystal structure of Ub-conjugated Ube2K C92K&K97A mutant (isopeptide linkage), 2.1 A…
3F92 2.23 Å, Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington Interacting…
7MYH 2.39 Å, Ubiquitin variant UbV.k.2 in complex with Ube2k
1YLA 2.4 Å, Ubiquitin-conjugating enzyme E2-25 kDa (Huntington interacting protein 2)
7OJX 2.4 Å, E2 UBE2K covalently linked to donor Ub, acceptor di-Ub, and RING E3 primed for…
6IF1 2.47 Å, Crystal structure of Ube2K and K48-linked di-ubiquitin complex
2O25 2.6 Å, Ubiquitin-Conjugating Enzyme E2-25 kDa Complexed With SUMO-1-Conjugating Enzyme UBC9
6JB6 2.7 Å, Crystal structure of Ub-conjugated Ube2K C92K&K97A mutant (isopeptide linkage), 2.7 A…
3K9P 2.8 Å, The crystal structure of E2-25K and ubiquitin complex
7MYF 3.0 Å, Ubiquitin variant UbV.k.1 in complex with Ube2k

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