1YLA: Ubiquitin-conjugating enzyme E2-25 kDa

Ubiquitin-conjugating enzyme E2-25 kDa (Huntington interacting protein 2). Determined by X-ray diffraction at 2.4 Å resolution. Released 1 Feb 2005.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,308
Mol. weight: 45.15 kDa
Released: 1 Feb 2005

Explore 1YLA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1YLA contains 22 α-helices and 16 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: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-17	15
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
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	94-97	4
α-helix	106-118	13
α-helix	128-136	9
α-helix	138-153	16
α-helix	160-171	12
α-helix	176-185	10
α-helix	190-196	7

Chain B: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-17	15
α-helix	20-23	4
β-strand	29-31	3	3
β-strand	38-44	7	3
α-helix	45-46	2
β-strand	55-61	7	3
β-strand	72-75	4	3
β-strand	81	1	4
β-strand	84	1	4
β-strand	90	1	3
β-strand	91	1	4
α-helix	94-96	3
α-helix	106-118	13
α-helix	128-136	9
α-helix	138-148	11
α-helix	149-153	5
α-helix	155-157	3
α-helix	160-170	11
α-helix	176-185	10
α-helix	190-196	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2-25 kDa	A, B	protein	202	Homo sapiens	P61086 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1YLA_1 Ubiquitin-conjugating enzyme E2-25 kDa (chains A, B)
GSMANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQL
EIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLA
AAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNA
VIVALSSKSWDVETATELLLSN

Primary citation

Structural basis of E2-25K/UBB+1 interaction leading to proteasome inhibition and neurotoxicity. Ko, S., Kang, G.B., Song, S.M. et al. J Biol Chem (2010) 285:36070-36080. DOI 10.1074/jbc.M110.145219 · PubMed

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

3K9O 1.8 Å, The crystal structure of E2-25K and UBB+1 complex
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
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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