2LWP: The ubiquitin homology domain of mouse BAG-1

The NMR solution structure of the the ubiquitin homology domain of mouse BAG-1. Determined by solution NMR. Released 19 Jun 2013.

Method
Solution NMR
Organism
Mus musculus
Chains
1
Atoms
751
Mol. weight
10.8 kDa
Released
19 Jun 2013

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

Secondary structure: helices and β-sheets

2LWP contains 2 α-helices and 5 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: 2 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand19-2461
β-strand27-3261
α-helix44-5512
α-helix59-613
β-strand64-6631
β-strand69-7021
β-strand88-9141

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BAG family molecular chaperone regulator 1Aprotein97Mus musculusQ60739 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LWP_1 BAG family molecular chaperone regulator 1 (chains A)
MAKTEEMVQTEEMETPRLSVIVTHSNERYDLLVTPQQGNSEPVVQDLAQLVEEATGVPLP
FQKLIFKGKSLKEMETPLSALGMQNGCRVMLIGEKSN

Primary citation

The NMR solution structure of the ubiquitin homology domain of Bcl-2-associated athanogene 1 (BAG-1-UBH) from Mus musculus. Huang, H.W., Yu, C. Biochem Biophys Res Commun (2013) 431:86-91. DOI 10.1016/j.bbrc.2012.12.082 · PubMed

Other PDB entries of the same protein (UniProt Q60739 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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