2MT6: Human ubiquitin conjugating enzyme Ube2w

Solution structure of the human ubiquitin conjugating enzyme Ube2w. Determined by solution NMR. Released 26 Nov 2014.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 1,215
Mol. weight: 17.35 kDa
Released: 26 Nov 2014

Explore 2MT6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2MT6 contains 13 α-helices and 10 β-strands across 1 chain. 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: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-17	14
α-helix	19-20	2
β-strand	23-28	6	1
α-helix	29	1
β-strand	36-42	7	1
β-strand	43	1	2
α-helix	44	1
β-strand	50	1	2
β-strand	53-59	7	1
α-helix	60-61	2
α-helix	68-69	2
β-strand	70-74	5	1
α-helix	78-80	3
β-strand	81	1	3
β-strand	84	1	3
β-strand	89	1	1
β-strand	90	1	3
α-helix	93-95	3
α-helix	105-117	13
α-helix	119-122	4
α-helix	128-133	6
α-helix	135-137	3
α-helix	139-142	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 W	A	protein	151	Homo sapiens	Q96B02 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2MT6_1 Ubiquitin-conjugating enzyme E2 W (chains A)
MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKF
SSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCK
EKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC

Primary citation

Intrinsic disorder drives N-terminal ubiquitination by Ube2w. Vittal, V., Shi, L., Wenzel, D.M. et al. Nat Chem Biol (2015) 11:83-89. DOI 10.1038/nchembio.1700 · PubMed

Other PDB entries of the same protein (UniProt Q96B02 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2A7L 1.82 Å, Structure of the human hypothetical ubiquitin-conjugating enzyme, LOC55284
8A58 2.25 Å, X-ray structure of TRIM21 RING E3 ligase in complex with E2 enzyme Ube2W

Browse structure collections

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