2HLW: Human Ubiquitin-conjugating Enzyme Variant Uev1a

Solution Structure of the Human Ubiquitin-conjugating Enzyme Variant Uev1a. Determined by solution NMR. Released 5 Sept 2006.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,353
Mol. weight
19.33 kDa
Released
5 Sept 2006

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

Secondary structure: helices and β-sheets

2HLW contains 6 α-helices and 11 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: 6 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix36-4914
α-helix52-543
β-strand56-6051
β-strand7012
β-strand71-7551
α-helix77-782
β-strand8811
β-strand90-9342
β-strand104-10742
β-strand10913
β-strand11614
β-strand12212
β-strand12314
α-helix129-1324
α-helix140-15213
α-helix160-1623
β-strand16713

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-conjugating enzyme E2 variant 1Aprotein170Homo sapiensQ13404 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2HLW_1 Ubiquitin-conjugating enzyme E2 variant 1 (chains A)
MPGEVQASYLKSQSKLSDEGRLEPRKFHCKGVKVPRNFRLLEELEEGQKGVGDGTVSWGL
EDDEDMTLTRWTGMIIGPPRTIYENRIYSLKIECGPKYPEAPPFVRFVTKINMNGVNSSN
GVVDPRAISVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQCYSN

Primary citation

Structure and interactions of the ubiquitin-conjugating enzyme variant human uev1a: implications for enzymatic synthesis of polyubiquitin chains(,). Hau, D.D., Lewis, M.J., Saltibus, L.F. et al. Biochemistry (2006) 45:9866-9877. DOI 10.1021/bi060631r · PubMed

Other PDB entries of the same protein (UniProt Q13404 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2HLW 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.