2MP2: SUMO dimer

Solution structure of SUMO dimer in complex with SIM2-3 from RNF4. Determined by solution NMR. Released 2 Jul 2014.

Method: Solution NMR
Organisms: Homo sapiens, Mus musculus
Chains: 3
Atoms: 1,566
Mol. weight: 22.42 kDa
Released: 2 Jul 2014

Explore 2MP2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2MP2 contains 4 α-helices and 10 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: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	18-22	5	1
α-helix	30-39	10
β-strand	48-51	4	1
β-strand	54	1	1
α-helix	63-65	3
β-strand	71-76	6	1

Chain B: 2 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	17-23	7	2
β-strand	29-33	5	2
α-helix	40-50	11
β-strand	61	1	3
β-strand	64	1	3
α-helix	72-75	4
β-strand	81-85	5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Small ubiquitin-related modifier 3	A	protein	82	Homo sapiens	P55854 (AlphaFold model)
Small ubiquitin-related modifier 3	B	protein	90	Homo sapiens	P55854 (AlphaFold model)
E3 ubiquitin-protein ligase RNF4	C	protein	25	Mus musculus	Q9QZS2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2MP2_1 Small ubiquitin-related modifier 3 (chains A)
GTENDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETD
TPAQLEMEDEDTIDVFQQQTGG

Sequence of entity 2 (B), FASTA

>2MP2_2 Small ubiquitin-related modifier 3 (chains B)
GSEEKPKEGVKTENDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFR
FDGQPINETDTPAQLEMEDEDTIDVFQQQT

Sequence of entity 3 (C), FASTA

>2MP2_3 E3 ubiquitin-protein ligase RNF4 (chains C)
TVGDEIVDLTCESLEPVVVDLTHND

Primary citation

Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4. Xu, Y., Plechanovova, A., Simpson, P. et al. Nat Commun (2014) 5:4217-4217. DOI 10.1038/ncomms5217 · PubMed

Other PDB entries of the same protein (UniProt P55854 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7R2E 1.74 Å, Structure of human Senp7 with SUMO2
7ZJU 2.17 Å, Structure of human USPL1 in covalent complex with SUMO3-2Br probe
9GNN 2.36 Å, Structure of SENP5 in complex with SUMO2
2IO1 2.6 Å, Crystal structure of human Senp2 in complex with preSUMO-3
6NNQ 2.62 Å, Non-covalent structure of SENP1 in complex with SUMO2
1U4A Solution structure of human SUMO-3 C47S
6K5R Complex of SUMO2 with Phosphorylated viral SIM IE2

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