The crystal structure of MBTD1. Determined by X-ray diffraction at 2.5 Å resolution. Released 6 Jan 2009.
Explore 3FEO in 3D Show helices and sheets RCSB PDB PDBe
3FEO contains 41 α-helices and 55 β-strands across 2 chains. 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 | 14-21 | 8 | |
| β-strand | 25 | 1 | 1 |
| α-helix | 26-27 | 2 | |
| α-helix | 28-30 | 3 | |
| β-strand | 48-52 | 5 | 2 |
| β-strand | 63-72 | 10 | 2 |
| β-strand | 75-80 | 6 | 2 |
| β-strand | 91-94 | 4 | 2 |
| β-strand | 101-102 | 2 | 2 |
| α-helix | 105-109 | 5 | |
| α-helix | 111-112 | 2 | |
| β-strand | 113 | 1 | 2 |
| α-helix | 117-119 | 3 | |
| α-helix | 126-134 | 9 | |
| α-helix | 144-151 | 8 | |
| β-strand | 160-166 | 7 | 3 |
| β-strand | 169-182 | 14 | 3 |
| β-strand | 185-190 | 6 | 3 |
| β-strand | 199-203 | 5 | 3 |
| β-strand | 209-210 | 2 | 3 |
| α-helix | 214-218 | 5 | |
| β-strand | 222 | 1 | 3 |
| β-strand | 235-236 | 2 | 3 |
| α-helix | 239-241 | 3 | |
| α-helix | 243-247 | 5 | |
| β-strand | 260-265 | 6 | 4 |
| β-strand | 268-280 | 13 | 4 |
| α-helix | 282-284 | 3 | |
| β-strand | 285-290 | 6 | 4 |
| β-strand | 302-305 | 4 | 4 |
| β-strand | 311-312 | 2 | 4 |
| α-helix | 316-320 | 5 | |
| α-helix | 323 | 1 | |
| β-strand | 324-325 | 2 | 4 |
| α-helix | 326-327 | 2 | |
| α-helix | 337-344 | 8 | |
| β-strand | 348 | 1 | 4 |
| α-helix | 349-350 | 2 | |
| α-helix | 351-354 | 4 | |
| β-strand | 368-372 | 5 | 1 |
| β-strand | 380-389 | 10 | 1 |
| β-strand | 392-397 | 6 | 1 |
| α-helix | 402-404 | 3 | |
| β-strand | 406-409 | 4 | 1 |
| β-strand | 415-416 | 2 | 1 |
| α-helix | 420-424 | 5 | |
| α-helix | 426-427 | 2 | |
| β-strand | 428-429 | 2 | 1 |
| α-helix | 430-431 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-21 | 8 | |
| β-strand | 25 | 1 | 5 |
| α-helix | 26-27 | 2 | |
| α-helix | 28-30 | 3 | |
| β-strand | 48-52 | 5 | 6 |
| β-strand | 63-72 | 10 | 6 |
| β-strand | 75-80 | 6 | 6 |
| β-strand | 91-94 | 4 | 6 |
| β-strand | 101-102 | 2 | 6 |
| β-strand | 113 | 1 | 6 |
| α-helix | 117-119 | 3 | |
| α-helix | 126-134 | 9 | |
| α-helix | 144-151 | 8 | |
| β-strand | 160-165 | 6 | 7 |
| β-strand | 172 | 1 | 8 |
| β-strand | 173-182 | 10 | 7 |
| β-strand | 185-190 | 6 | 7 |
| β-strand | 201-203 | 3 | 7 |
| β-strand | 209-210 | 2 | 7 |
| α-helix | 214-218 | 5 | |
| β-strand | 221 | 1 | 8 |
| β-strand | 235-236 | 2 | 7 |
| α-helix | 237-238 | 2 | |
| α-helix | 239-241 | 3 | |
| α-helix | 244-246 | 3 | |
| β-strand | 260-265 | 6 | 9 |
| β-strand | 268-280 | 13 | 9 |
| β-strand | 285-290 | 6 | 9 |
| β-strand | 302-305 | 4 | 9 |
| β-strand | 311-312 | 2 | 9 |
| α-helix | 316-319 | 4 | |
| β-strand | 324-325 | 2 | 9 |
| α-helix | 326-327 | 2 | |
| α-helix | 335 | 1 | |
| α-helix | 337-343 | 7 | |
| β-strand | 348 | 1 | 9 |
| α-helix | 349-350 | 2 | |
| α-helix | 351-354 | 4 | |
| β-strand | 368-372 | 5 | 5 |
| β-strand | 380-389 | 10 | 5 |
| β-strand | 392-397 | 6 | 5 |
| α-helix | 402-404 | 3 | |
| β-strand | 406-409 | 4 | 5 |
| β-strand | 415-416 | 2 | 5 |
| α-helix | 420-424 | 5 | |
| β-strand | 429 | 1 | 5 |
| α-helix | 430-431 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MBT domain-containing protein 1 | A, B | protein | 437 | Homo sapiens | Q05BQ5 (AlphaFold model) |
>3FEO_1 MBT domain-containing protein 1 (chains A, B) AKTKAAVSMEGFSWGNYINSNSFIAAPVTCFKHAPMGTCWGDISENVRVEVPNTDCSLPT KVFWIAGIVKLAGYNALLRYEGFENDSGLDFWCNICGSDIHPVGWCAASGKPLVPPRTIQ HKYTNWKAFLVKRLTGAKTLPPDFSQKVSESMQYPFKPCMRVEVVDKRHLCRTRVAVVES VIGGRLRLVYEESEDRTDDFWCHMHSPLIHHIGWSRSIGHRFKRSDITKKQDGHFDTPPH LFAKVKEVDQSGEWFKEGMKLEAIDPLNLSTICVATIRKVLADGFLMIGIDGSEAADGSD WFCYHATSPSIFPVGFCEINMIELTPPRGYTKLPFKWFDYLRETGSIAAPVKLFNKDVPN HGFRVGMKLEAVDLMEPRLICVATVTRIIHRLLRIHFDGWEEEYDQWVDCESPDLYPVGW CQLTGYQLQPPASQSSR
Structural studies of a four-MBT repeat protein MBTD1. Eryilmaz, J., Pan, P., Amaya, M.F. et al. PLoS One (2009) 4:e7274-e7274. DOI 10.1371/journal.pone.0007274 · PubMed
Other PDB entries of the same protein (UniProt Q05BQ5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3FEO 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.