Crystal structure of human MOF in complex with MSL1. Determined by X-ray diffraction at 2.05 Å resolution. Released 25 Jul 2012.
Explore 4DNC in 3D Show helices and sheets RCSB PDB PDBe
4DNC contains 28 α-helices and 34 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 181-184 | 4 | 1 |
| β-strand | 187-190 | 4 | 1 |
| α-helix | 201-203 | 3 | |
| β-strand | 206-209 | 4 | 1 |
| β-strand | 216-217 | 2 | 1 |
| α-helix | 220-229 | 10 | |
| β-strand | 238-243 | 6 | 2 |
| β-strand | 246-252 | 7 | 2 |
| α-helix | 257-268 | 12 | |
| β-strand | 283-291 | 9 | 2 |
| β-strand | 296-305 | 10 | 2 |
| β-strand | 312-314 | 3 | 3 |
| β-strand | 317-319 | 3 | 2 |
| α-helix | 321-323 | 3 | |
| α-helix | 328-342 | 15 | |
| β-strand | 347 | 1 | 4 |
| β-strand | 348-349 | 2 | 3 |
| α-helix | 350 | 1 | |
| α-helix | 352 | 1 | |
| α-helix | 355-375 | 21 | |
| α-helix | 382-389 | 8 | |
| β-strand | 391 | 1 | 4 |
| α-helix | 393-402 | 10 | |
| β-strand | 406-409 | 4 | 5 |
| β-strand | 412-415 | 4 | 5 |
| α-helix | 419-427 | 9 | |
| α-helix | 440-442 | 3 | |
| β-strand | 443 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 181-184 | 4 | 6 |
| β-strand | 187-190 | 4 | 6 |
| α-helix | 199-203 | 5 | |
| β-strand | 206-209 | 4 | 6 |
| β-strand | 216-217 | 2 | 6 |
| α-helix | 220-229 | 10 | |
| β-strand | 238-243 | 6 | 7 |
| β-strand | 246-252 | 7 | 7 |
| α-helix | 257-268 | 12 | |
| β-strand | 283-292 | 10 | 7 |
| β-strand | 295-305 | 11 | 7 |
| β-strand | 312-314 | 3 | 8 |
| β-strand | 317-319 | 3 | 7 |
| α-helix | 321-323 | 3 | |
| α-helix | 328-342 | 15 | |
| β-strand | 347 | 1 | 9 |
| β-strand | 348-349 | 2 | 8 |
| α-helix | 350 | 1 | |
| α-helix | 352 | 1 | |
| α-helix | 355-375 | 21 | |
| α-helix | 382-389 | 8 | |
| β-strand | 391 | 1 | 9 |
| α-helix | 393-402 | 10 | |
| β-strand | 406-407 | 2 | 10 |
| β-strand | 414-415 | 2 | 10 |
| α-helix | 419-427 | 9 | |
| α-helix | 429-431 | 3 | |
| α-helix | 432-434 | 3 | |
| α-helix | 440-442 | 3 | |
| β-strand | 443 | 1 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 478-480 | 3 | 1 |
| α-helix | 546-564 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 478-480 | 3 | 6 |
| α-helix | 546-563 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone acetyltransferase KAT8 | A, B | protein | 289 | Homo sapiens | Q9H7Z6 (AlphaFold model) |
| Male-specific lethal 1 homolog | D, E | protein | 48 | Homo sapiens | Q68DK7 (AlphaFold model) |
>4DNC_1 Histone acetyltransferase KAT8 (chains A, B) HEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQ CQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILT EVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSP EKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYW KGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPKHKQVKLSKK
>4DNC_2 Male-specific lethal 1 homolog (chains D, E) LAVPSWRDHSVEPLRDPNPSDLLENLDDSVFSKRHAKLELDEKRRKRW
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex. Huang, J., Wan, B., Wu, L. et al. Cell Res (2012) 22:1078-1081. DOI 10.1038/cr.2012.72 · PubMed
Other PDB entries of the same protein (UniProt Q9H7Z6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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