2PE6: SUMO-conjugating enzyme UBC9

Non-covalent complex between human SUMO-1 and human Ubc9. Determined by X-ray diffraction at 2.4 Å resolution. Released 17 Apr 2007.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,960
Mol. weight: 29.46 kDa
Released: 17 Apr 2007

Explore 2PE6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2PE6 contains 12 α-helices and 12 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: 9 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	3-18	16
β-strand	25-30	6	1
α-helix	31	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	74-77	4	1
α-helix	80-81	2
β-strand	86	1	2
β-strand	91	1	1
β-strand	92	1	2
α-helix	95-97	3
α-helix	109-121	13
α-helix	131-139	9
α-helix	141-154	14

Chain B: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	22-28	7	3
β-strand	34-38	5	3
α-helix	44-55	12
α-helix	59-61	3
β-strand	62-66	5	3
β-strand	69-70	2	3
α-helix	71-72	2
β-strand	86-92	7	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SUMO-conjugating enzyme UBC9	A	protein	161	Homo sapiens	P63279 (AlphaFold model)
Small ubiquitin-related modifier 1	B	protein	97	Homo sapiens	P63165 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2PE6_1 SUMO-conjugating enzyme UBC9 (chains A)
GSHMSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGL
FKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQ
ELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS

Sequence of entity 2 (B), FASTA

>2PE6_2 Small ubiquitin-related modifier 1 (chains B)
MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMN
SLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGG

Primary citation

Structure and Analysis of a Complex between SUMO and Ubc9 Illustrates Features of a Conserved E2-Ubl Interaction. Capili, A.D., Lima, C.D. J Mol Biol (2007) 369:608-618. DOI 10.1016/j.jmb.2007.04.006 · PubMed

Other PDB entries of the same protein (UniProt P63279 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5F6E 1.12 Å, Crystal Structure of human Ubc9 (K48A/K49A/E54A)
5F6Y 1.14 Å, Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 2 (mercaptobenzoxazole)
2GRR 1.3 Å, Crystal Structure of human RanGAP1-Ubc9-D127S
5F6V 1.49 Å, Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 1 (biphenol from…
5F6U 1.55 Å, Crystal Structure of Ubc9 (K48A/K49A/E54A) complexed with Fragment 8 (JSS190B146)
5F6D 1.55 Å, Crystal structure of Ubc9 (K48A/K49A/E54A) complexed with Fragment 6
5F6X 1.56 Å, Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 2 (mercaptobenzoxazole…
5F6W 1.7 Å, Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 1 (biphenol)
2GRO 1.7 Å, Crystal Structure of human RanGAP1-Ubc9-N85Q
2GRQ 1.7 Å, Crystal Structure of human RanGAP1-Ubc9-D127A
9GLR 1.72 Å, Crystal Structure of Human UBC9 C93E
2GRN 1.8 Å, Crystal Structure of human RanGAP1-Ubc9

Browse structure collections

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