6D68: Ube2G1

Ube2G1 in complex with ubiquitin variant Ubv.G1.1. Determined by X-ray diffraction at 2.36 Å resolution. Released 17 Jul 2019.

Method: X-ray diffraction
Resolution: 2.36 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,758
Mol. weight: 59.22 kDa
Released: 17 Jul 2019

Explore 6D68 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6D68 contains 21 α-helices and 28 β-strands across 4 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, 7 β-strands

Element	Residues	Length	Sheet
α-helix	1-19	19
α-helix	21-22	2
β-strand	25-29	5	1
β-strand	37-43	7	1
α-helix	44-45	2
β-strand	54-60	7	1
β-strand	71-74	4	1
β-strand	83	1	2
β-strand	88	1	1
β-strand	89	1	2
α-helix	92-94	3
α-helix	117-129	13
α-helix	139-147	9
α-helix	149-153	5
α-helix	154-168	15

Chain B: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	4-19	16
α-helix	21-22	2
β-strand	25-31	7	3
β-strand	34-43	10	3
α-helix	44-45	2
β-strand	54-60	7	3
β-strand	71-74	4	3
β-strand	83	1	4
β-strand	88	1	3
β-strand	89	1	4
α-helix	92-94	3
α-helix	117-129	13
α-helix	139-147	9
α-helix	149-153	5
α-helix	154-168	15

Chain C: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	1-7	7	5
β-strand	13-17	5	6
β-strand	22	1	7
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	6
β-strand	48-49	2	6
β-strand	55	1	7
β-strand	66-71	6	6

Chain D: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	1-7	7	6
β-strand	13-17	5	5
β-strand	22	1	8
α-helix	23-34	12
α-helix	38-40	3
β-strand	41-45	5	5
β-strand	48-49	2	5
β-strand	55	1	8
α-helix	57-59	3
β-strand	66-71	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 G1	A, B	protein	171	Homo sapiens	P62253 (AlphaFold model)
Ubv.G1.1	C, D	protein	86	Homo sapiens	Q96H31 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6D68_1 Ubiquitin-conjugating enzyme E2 G1 (chains A, B)
SMTELQSALLLRRQLAELNKNPVEGFSAGLIDDNDLYRWEVLIIGPPDTLYEGGVFKAHL
TFPKDYPLRPPKMKFITEIWHPNVDKNGDVCISILHEPGEDKYGYEKPEERWLPIHTVET
IMISVISMLADPNGDSPANVDAAKEWREDRNGEFKRKVARCVRKSQETAFE

Sequence of entity 2 (C, D), FASTA

>6D68_2 Ubv.G1.1 (chains C, D)
GAGGDYKDDDDKMQIFVKPIRVKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFSGK
LLEDGRTLSDYNIQKEYTLHLLLRRH

Primary citation

Structural and Functional Analysis of Ubiquitin-based Inhibitors That Target the Backsides of E2 Enzymes. Garg, P., Ceccarelli, D.F., Keszei, A.F.A. et al. J Mol Biol (2020) 432:952-966. DOI 10.1016/j.jmb.2019.09.024 · PubMed

Other PDB entries of the same protein (UniProt P62253 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2AWF 2.1 Å, Structure of human Ubiquitin-conjugating enzyme E2 G1

Browse structure collections

About this viewer

MolViewer shows 6D68 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.