Solution structure of the tandem HMG box domain from Human High mobility group protein B1. Determined by solution NMR. Released 12 Feb 2008.
Explore 2YRQ in 3D Show helices and sheets RCSB PDB PDBe
2YRQ contains 9 α-helices and 0 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 | 22-37 | 16 | |
| α-helix | 45-58 | 14 | |
| α-helix | 61-77 | 17 | |
| α-helix | 79-84 | 6 | |
| α-helix | 102-106 | 5 | |
| α-helix | 108-123 | 16 | |
| α-helix | 129-142 | 14 | |
| α-helix | 145-147 | 3 | |
| α-helix | 148-170 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| High mobility group protein B1 | A | protein | 173 | Homo sapiens | P09429 (AlphaFold model) |
>2YRQ_1 High mobility group protein B1 (chains A) GSSGSSGMGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMS AKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKI KGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKG
Solution structure of the tandem HMG box domain from Human High mobility group protein B1. Tomizawa, T., Koshiba, S., Watanabe, S. et al. To be published.
Other PDB entries of the same protein (UniProt P09429 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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