3ONG: Ubiquitin-activating enzyme E1-like

Crystal structure of UBA2ufd-Ubc9: insights into E1-E2 interactions in Sumo pathways. Determined by X-ray diffraction at 2.3 Å resolution. Released 12 Jan 2011.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 4,305
Mol. weight: 64.81 kDa
Released: 12 Jan 2011

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

Secondary structure: helices and β-sheets

3ONG contains 24 α-helices and 36 β-strands across 4 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: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	442-448	7	1
α-helix	450-453	4
β-strand	457	1	2
α-helix	458-469	12
β-strand	475-479	5	1
β-strand	484-488	5	1
β-strand	498	1	2
α-helix	499-502	4
β-strand	508-514	7	1
β-strand	520-522	3	3
α-helix	523-524	2
β-strand	525-531	7	1
β-strand	540-541	2	1
α-helix	547-548	2
β-strand	549-551	3	3

Chain B: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
β-strand	25-30	6	4
β-strand	36-46	11	4
α-helix	47-48	2
β-strand	56	1	5
β-strand	57-63	7	4
β-strand	74-76	3	4
α-helix	77-78	2
β-strand	86	1	6
β-strand	91	1	4
β-strand	92	1	6
α-helix	95-97	3
α-helix	109-121	13
α-helix	131-139	9
α-helix	141-154	14
β-strand	156	1	5

Chain C: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	442-448	7	4
α-helix	452-455	4
β-strand	457	1	7
α-helix	458-468	11
β-strand	475-479	5	4
β-strand	484-488	5	4
β-strand	498	1	7
α-helix	499-502	4
β-strand	509-514	6	4
β-strand	521-522	2	8
α-helix	523-524	2
β-strand	525-531	7	4
α-helix	536	1
β-strand	540-541	2	4
β-strand	549-550	2	8

Chain D: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
β-strand	25-30	6	1
β-strand	36-46	11	1
α-helix	47-48	2
β-strand	57-63	7	1
α-helix	72-73	2
β-strand	74-76	3	1
β-strand	86	1	9
β-strand	91	1	1
β-strand	92	1	9
α-helix	95-97	3
α-helix	109-120	12
α-helix	131-139	9
α-helix	141-154	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-activating enzyme E1-like	A, C	protein	127	Saccharomyces cerevisiae	P52488 (AlphaFold model)
SUMO-conjugating enzyme UBC9	B, D	protein	159	Saccharomyces cerevisiae	P50623 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>3ONG_1 Ubiquitin-activating enzyme E1-like (chains A, C)
GSSKVCRGVIKLSSDCLNKMKLSDFVVLIREKYSYPQDISLLDASNQRLLFDYDFEDLND
RTLSEINLGNGSIILFSDEEGDTMIRKAIELFLDVDDELPCNTCSLPDVEVPLIKANNSP
SKNEEEE

Sequence of entity 2 (B, D), FASTA

>3ONG_2 SUMO-conjugating enzyme UBC9 (chains B, D)
GSMSSLCLQRLQEERKKWRKDHPFGFYAKPVKKADGSMDLQKWEAGIPGKEGTNWAGGVY
PITVEYPNEYPSKPPKVKFPAGFYHPNVYPSGTICLSILNEDQDWRPAITLKQIVLGVQD
LLDSPNPNSPAQEPAWRSFSRNKAEYDKKVLLQAKQYSK

Primary citation

Crystal structure of UBA2(ufd)-Ubc9: insights into E1-E2 interactions in Sumo pathways. Wang, J., Taherbhoy, A.M., Hunt, H.W. et al. PLoS One (2010) 5:e15805-e15805. DOI 10.1371/journal.pone.0015805 · PubMed

Other PDB entries of the same protein (UniProt P52488 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3ONH 1.6 Å, Crystal structure of UBA2ufd-Ubc9: insights into E1-E2 interactions in Sumo pathways

Browse structure collections

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