Cryo-EM structure of full-length MICAL1 in the autoinhibited state. Determined by electron microscopy at 3.94 Å resolution. Released 28 Aug 2024.
Explore 8Y6K in 3D Show helices and sheets RCSB PDB PDBe
8Y6K contains 31 α-helices and 31 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 | 9-18 | 10 | |
| α-helix | 23-35 | 13 | |
| α-helix | 46-51 | 6 | |
| α-helix | 58-60 | 3 | |
| α-helix | 61-71 | 11 | |
| α-helix | 74-79 | 6 | |
| β-strand | 86 | 1 | 1 |
| β-strand | 89-90 | 2 | 2 |
| α-helix | 94-105 | 12 | |
| β-strand | 109 | 1 | 1 |
| β-strand | 111-114 | 4 | 2 |
| β-strand | 124-126 | 3 | 3 |
| α-helix | 129-136 | 8 | |
| β-strand | 154-156 | 3 | 3 |
| α-helix | 157-170 | 14 | |
| β-strand | 174-177 | 4 | 2 |
| β-strand | 180-185 | 6 | 4 |
| α-helix | 186-187 | 2 | |
| β-strand | 194 | 1 | 5 |
| β-strand | 195-199 | 5 | 4 |
| α-helix | 204-207 | 4 | |
| β-strand | 211 | 1 | 5 |
| β-strand | 213-216 | 4 | 2 |
| β-strand | 229-232 | 4 | 6 |
| β-strand | 238-245 | 8 | 7 |
| α-helix | 250-253 | 4 | |
| β-strand | 261 | 1 | 7 |
| α-helix | 267-277 | 11 | |
| β-strand | 283-287 | 5 | 7 |
| β-strand | 291-298 | 8 | 7 |
| α-helix | 300-305 | 6 | |
| β-strand | 309 | 1 | 8 |
| α-helix | 316-319 | 4 | |
| β-strand | 325 | 1 | 8 |
| α-helix | 327-341 | 15 | |
| β-strand | 360-365 | 6 | 7 |
| β-strand | 369-372 | 4 | 6 |
| β-strand | 376-381 | 6 | 2 |
| β-strand | 384-390 | 7 | 2 |
| β-strand | 396 | 1 | 6 |
| α-helix | 400-402 | 3 | |
| α-helix | 405-424 | 20 | |
| α-helix | 429-443 | 15 | |
| α-helix | 462-464 | 3 | |
| α-helix | 476-479 | 4 | |
| β-strand | 484 | 1 | 2 |
| α-helix | 510-520 | 11 | |
| α-helix | 541-550 | 10 | |
| α-helix | 557-561 | 5 | |
| α-helix | 565-579 | 15 | |
| α-helix | 582-584 | 3 | |
| α-helix | 588-593 | 6 | |
| α-helix | 597-610 | 14 | |
| β-strand | 696 | 1 | 9 |
| β-strand | 703 | 1 | 9 |
| α-helix | 706-708 | 3 | |
| β-strand | 709-711 | 3 | 10 |
| β-strand | 716-718 | 3 | 10 |
| β-strand | 736 | 1 | 11 |
| β-strand | 747 | 1 | 11 |
| α-helix | 915-958 | 44 | |
| α-helix | 964-1007 | 44 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| [F-actin]-monooxygenase MICAL1 | A | protein | 1067 | Homo sapiens | Q8TDZ2 (AlphaFold model) |
>8Y6K_1 [F-actin]-monooxygenase MICAL1 (chains A) MASPTSTNPAHAHFESFLQAQLCQDVLSSFQELCGALGLEPGGGLPQYHKIKDQLNYWSA KSLWTKLDKRAGQPVYQQGRACTSTKCLVVGAGPCGLRVAVELALLGARVVLVEKRTKFS RHNVLHLWPFTIHDLRALGAKKFYGRFCTGTLDHISIRQLQLLLLKVALLLGVEIHWGVT FTGLQPPPRKGSGWRAQLQPNPPAQLANYEFDVLISAAGGKFVPEGFKVREMRGKLAIGI TANFVNGRTVEETQVPEISGVARIYNQSFFQSLLKATGIDLENIVYYKDDTHYFVMTAKK QCLLRLGVLRQDWPDTNRLLGSANVVPEALQRFTRAAADFATHGKLGKLEFAQDAHGQPD VSAFDFTSMMRAESSARVQEKHGARLLLGLVGDCLVEPFWPLGTGVARGFLAAFDAAWMV KRWAEGAESLEVLAERESLYQLLSQTSPENMHRNVAQYGLDPATRYPNLNLRAVTPNQVR DLYDVLAKEPVQRNNDKTDTGMPATGSAGTQEELLRWCQEQTAGYPGVHVSDLSSSWADG LALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQAVVAGSDPLGL IAYLSHFHSAFKSMAHSPGPVSQASPGTSSAVLFLSKLQRTLQRSRAKENAEDAGGKKLR LEMEAETPSTEVPPDPEPGVPLTPPSQHQEAGAGDLCALCGEHLYVLERLCVNGHFFHRS CFRCHTCEATLWPGGYEQHPGDGHFYCLQHLPQTDHKAEGSDRGPESPELPTPSENSMPP GLSTPTASQEGAGPVPDPSQPTRRQIRLSSPERQRLSSLNLTPDPEMEPPPKPPRSCSAL ARHALESSFVGWGLPVQSPQALVAMEKEEKESPFSSEEEEEDVPLDSDVEQALQTFAKTS GTMNNYPTWRRTLLRRAKEEEMKRFCKAQTIQRRLNEIEAALRELEAEGVKLELALRRQS SSPEQQKKLWVGQLLQLVDKKNSLVAEEAELMITVQELNLEEKQWQLDQELRGYMNREEN LKTAADRQAEDQVLRKLVDLVNQRDALIRFQEERRLSELALGTGAQG
Autoinhibition and relief mechanisms for MICAL monooxygenases in F-actin disassembly. Lin, L., Dong, J., Xu, S. et al. Nat Commun (2024) 15:6824-6824. DOI 10.1038/s41467-024-50940-7 · PubMed
Other PDB entries of the same protein (UniProt Q8TDZ2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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