2LXH: RING domain in ubiquitin ligase gp78

NMR structure of the RING domain in ubiquitin ligase gp78. Determined by solution NMR. Released 28 Aug 2013.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
448
Mol. weight
9.37 kDa
Ligands
ZN
Released
28 Aug 2013

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

Secondary structure: helices and β-sheets

2LXH contains 2 α-helices and 4 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 C: 2 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix332-3376
β-strand352-35321
β-strand359-36021
α-helix362-37110
β-strand37412
β-strand38112

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
E3 ubiquitin-protein ligase AMFRCprotein81Homo sapiensQ9UKV5 (AlphaFold model)
Sequence of entity 1 (C), FASTA
>2LXH_1 E3 ubiquitin-protein ligase AMFR (chains C)
KNYLRVVGNMEARFAVATPEELAVNNDDCAICWDSMQAARKLPCGHLFHNSCLRSWLEQD
TSCPTCRMSLNIADNNRVREE

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

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 Q9UKV5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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