Solution Structure of the Human Ubiquitin-conjugating Enzyme Variant Uev1a. Determined by solution NMR. Released 5 Sept 2006.
Explore 2HLW in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-49 | 14 | |
| α-helix | 52-54 | 3 | |
| β-strand | 56-60 | 5 | 1 |
| β-strand | 70 | 1 | 2 |
| β-strand | 71-75 | 5 | 1 |
| α-helix | 77-78 | 2 | |
| β-strand | 88 | 1 | 1 |
| β-strand | 90-93 | 4 | 2 |
| β-strand | 104-107 | 4 | 2 |
| β-strand | 109 | 1 | 3 |
| β-strand | 116 | 1 | 4 |
| β-strand | 122 | 1 | 2 |
| β-strand | 123 | 1 | 4 |
| α-helix | 129-132 | 4 | |
| α-helix | 140-152 | 13 | |
| α-helix | 160-162 | 3 | |
| β-strand | 167 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-conjugating enzyme E2 variant 1 | A | protein | 170 | Homo sapiens | Q13404 (AlphaFold model) |
>2HLW_1 Ubiquitin-conjugating enzyme E2 variant 1 (chains A) MPGEVQASYLKSQSKLSDEGRLEPRKFHCKGVKVPRNFRLLEELEEGQKGVGDGTVSWGL EDDEDMTLTRWTGMIIGPPRTIYENRIYSLKIECGPKYPEAPPFVRFVTKINMNGVNSSN GVVDPRAISVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQCYSN
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:
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.