5EQL: SUMO-Affirmer-S2D5

Isoform-specific inhibition of SUMO-dependent protein-protein interactions. Determined by X-ray diffraction at 2.49 Å resolution. Released 23 Nov 2016.

Method: X-ray diffraction
Resolution: 2.49 Å
Organisms: synthetic construct, Homo sapiens
Chains: 2
Atoms: 1,235
Mol. weight: 22.22 kDa
Released: 23 Nov 2016

Explore 5EQL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5EQL contains 3 α-helices and 9 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: 1 helix, 4 β-strands

Element	Residues	Length	Sheet
α-helix	35-52	18
β-strand	57-69	13	1
β-strand	76-87	12	1
β-strand	90-101	12	1
β-strand	114-120	7	1

Chain B: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	17-24	8	1
β-strand	29-35	7	1
α-helix	41-51	11
α-helix	55-57	3
β-strand	58-62	5	1
β-strand	65-66	2	1
β-strand	82-88	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SUMO-Affirmer-S2D5	A	protein	116	synthetic construct
Small ubiquitin-related modifier 2	B	protein	77	Homo sapiens	P61956 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5EQL_1 SUMO-Affirmer-S2D5 (chains A)
MASAATGVRAVPGNENSLEIEELARFAVDEHNKKENALLEFVRVVKAKEQIDLTQEWVFT
MYYLTLEAKDGGKKKLYEAKVWVKGLTNWKLGMNFKELQEFKPVGDAAAAHHHHHH

Sequence of entity 2 (B), FASTA

>5EQL_2 Small ubiquitin-related modifier 2 (chains B)
MNNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDT
PAQLEMEDEDTIDVFQQ

Primary citation

Generation of specific inhibitors of SUMO-1- and SUMO-2/3-mediated protein-protein interactions using Affimer (Adhiron) technology. Hughes, D.J., Tiede, C., Penswick, N. et al. Sci Signal (2017) 10. DOI 10.1126/scisignal.aaj2005 · PubMed

Other PDB entries of the same protein (UniProt P61956 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1WM3 1.2 Å, Crystal structure of human SUMO-2 protein
1WM2 1.6 Å, Crystal structure of human SUMO-2 protein
4NPN 1.63 Å, Crystal structure of human tetra-SUMO-2
7P99 1.8 Å, Structure of human USPL1 in complex with SUMO2
2D07 2.1 Å, Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase
4BKG 2.11 Å, crystal structure of human diSUMO-2
3ZO5 2.15 Å, Structure of SENP2-Loop1 in complex with preSUMO-2
2IO0 2.3 Å, Crystal structure of human Senp2 in complex with preSUMO-2
5ELU 2.35 Å, Isoform-specific inhibition of SUMO-dependent protein-protein interactions
5D2M 2.4 Å, Complex between human SUMO2-RANGAP1, UBC9 and ZNF451
7ZJV 2.4 Å, Structure of human USPL1 in covalent complex with DeltaN-SUMO2/3-PA probe
3UIN 2.6 Å, Complex between human RanGAP1-SUMO2, UBC9 and the IR1 domain from RanBP2

Browse structure collections

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