4ONN: Human Mms2/Ubc13 - BAY 11-7082

Crystal structure of human Mms2/Ubc13 - BAY 11-7082. Determined by X-ray diffraction at 1.5 Å resolution. Released 6 May 2015.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,562
Mol. weight: 35.59 kDa
Ligands: BY1
Released: 6 May 2015

Explore 4ONN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ONN contains 16 α-helices and 17 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: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	11-24	14
β-strand	31-35	5	1
β-strand	45-51	7	1
α-helix	52-53	2
β-strand	62-68	7	1
α-helix	77-78	2
β-strand	79-82	4	1
β-strand	84	1	2
β-strand	91	1	3
β-strand	97	1	1
β-strand	98	1	3
α-helix	100-102	3
α-helix	104-107	4
α-helix	115-125	11
α-helix	134-138	5
β-strand	142	1	2

Chain B: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	6-17	12
α-helix	19-20	2
β-strand	23-27	5	4
β-strand	34-40	7	4
α-helix	41-42	2
β-strand	51-57	7	4
α-helix	66-67	2
β-strand	68-71	4	4
β-strand	77	1	5
β-strand	80	1	5
β-strand	85	1	4
β-strand	86	1	5
α-helix	89-91	3
α-helix	101-113	13
α-helix	126-131	6
α-helix	133-147	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 variant 2	A	protein	153	Homo sapiens	Q15819 (AlphaFold model)
Ubiquitin-conjugating enzyme E2 N	B	protein	160	Homo sapiens	P61088 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4ONN_1 Ubiquitin-conjugating enzyme E2 variant 2 (chains A)
GPLGSPEFMAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIG
PPRTNYENRIYSLKVECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNS
YSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN

Sequence of entity 2 (B), FASTA

>4ONN_2 Ubiquitin-conjugating enzyme E2 N (chains B)
GPLGSPEFMAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTF
KLELFLPEEYPMAAPKVRFMTKIYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALL
SAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI

Ligands and cofactors

ID	Name	Formula	Copies
BY1	3-[(4-methylphenyl)sulfonyl]prop-2-enenitrile	C10 H9 N O2 S	1

Water and common crystallization additives (GOL) are not listed.

Primary citation

Covalent Inhibition of Ubc13 Affects Ubiquitin Signaling and Reveals Active Site Elements Important for Targeting. Hodge, C.D., Edwards, R.A., Markin, C.J. et al. ACS Chem Biol (2015) 10:1718-1728. DOI 10.1021/acschembio.5b00222 · PubMed

Other PDB entries of the same protein (UniProt Q15819 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ONL 1.35 Å, Crystal structure of human Mms2/Ubc13_D81N, R85S, A122V, N123P
4ONM 1.35 Å, Crystal structure of human Mms2/Ubc13 - NSC697923
9BIV 1.68 Å, Crystal Structure of Ubc13 with a New Active Site Loop Conformation
9LHJ 1.68 Å, UBE2N/UBE2V2 complexed with a covalent inhibitor
8WR5 1.7 Å, The Crystal Structure of Mms2 from Biortus
4NR3 1.8 Å, Crystal Structure of a human Mms2/Ubc13 L121G mutant
1J7D 1.85 Å, Crystal Structure of hMms2-hUbc13
1J74 1.9 Å, Crystal Structure of Mms2
4NRG 1.95 Å, Crystal Structure of a human Mms2/Ubc13 D118G mutant
9N1F 2.1 Å, Crystal Structure of the Ark2C-Ubc13~Ub-Mms2 complex
7BBD 2.2 Å, Crystal structure of monoubiquitinated TRIM21 RING (Ub-RING) In complex with ubiquitin…
4NRI 2.3 Å, Crystal Structure of a human Mms2/Ubc13 A122G mutant

Browse structure collections

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