2LXP: Ubiquitin-conjugating enzyme E2 G2

Name: PDB 2LXP: NMR structure of two domains in ubiquitin ligase gp78, RING and G2BR, bound to its conjugating enzyme Ube2g
Published: 2013-08-28
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: ligase

NMR structure of two domains in ubiquitin ligase gp78, RING and G2BR, bound to its conjugating enzyme Ube2g. Determined by solution NMR. Released 28 Aug 2013.

Method: Solution NMR
Organism: Homo sapiens
Chains: 3
Atoms: 1,915
Mol. weight: 28.42 kDa
Ligands: ZN
Released: 28 Aug 2013

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

Secondary structure: helices and β-sheets

2LXP contains 10 α-helices and 11 β-strands across 3 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: 7 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	4-16	13
α-helix	20-21	2
β-strand	24-30	7	1
β-strand	33-42	10	1
α-helix	43-44	2
β-strand	53-59	7	1
β-strand	70-73	4	1
β-strand	82	1	2
β-strand	87	1	1
β-strand	88	1	2
α-helix	91-93	3
α-helix	116-128	13
α-helix	138-146	9
α-helix	148-163	16

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	577-599	23

Chain C: 2 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	332-337	6
β-strand	351-354	4	3
β-strand	358-361	4	3
α-helix	362-371	10
β-strand	374-375	2	4
β-strand	380-381	2	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ubiquitin-conjugating enzyme E2 G2	A	protein	164	Homo sapiens	P60604 (AlphaFold model)
E3 ubiquitin-protein ligase AMFR	B	protein	27	Homo sapiens	Q9UKV5 (AlphaFold model)
E3 ubiquitin-protein ligase AMFR	C	protein	58	Homo sapiens	Q9UKV5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2LXP_1 Ubiquitin-conjugating enzyme E2 G2 (chains A)
AGTALKRLMAEYKQLTLNPPEGIVAGPMNEENFFEWEALIMGPEDTCFEFGVFPAILSFP
LDYPLSPPKMRFTCEMFHPNIYPDGRVCISILHAPGDDPMGYESSAERWSPVQSVEKILL
SVVSMLAEPNDESGANVDASKMWRDDREQFYKIAKQIVQKSLGL

Sequence of entity 2 (B), FASTA

>2LXP_2 E3 ubiquitin-protein ligase AMFR (chains B)
SADERQRMLVQRKDELLQQARKRFLNK

Sequence of entity 3 (C), FASTA

>2LXP_3 E3 ubiquitin-protein ligase AMFR (chains C)
AVATPEELAVNNDDCAICWDSMQAARKLPCGHLFHNSCLRSWLEQDTSCPTCRMSLNI

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine. Das, R., Liang, Y.H., Mariano, J. et al. EMBO J (2013) 32:2504-2516. DOI 10.1038/emboj.2013.174 · PubMed

Other PDB entries of the same protein (UniProt P60604 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7LEW 1.74 Å, Crystal structure of UBE2G2 in complex with the UBE2G2-binding region of AUP1
3H8K 1.8 Å, Crystal structure of Ube2g2 complxed with the G2BR domain of gp78 at 1.8-A resolution
8T0S 1.95 Å, Crystal structure of UBE2G2 adduct with phenethyl isothiocyanate (PEITC) at the Cys48…
4LAD 2.3 Å, Crystal Structure of the Ube2g2:RING-G2BR complex
2CYX 2.56 Å, Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)
2KLY Solution structure of human ubiquitin conjugating enzyme Ube2g2

Browse structure collections

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