CryoEM structure of human MICAL1. Determined by electron microscopy at 3.1 Å resolution. Released 20 Nov 2024.
Explore 9EWY in 3D Show helices and sheets RCSB PDB PDBe
9EWY contains 40 α-helices and 33 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 | 9-19 | 11 | |
| α-helix | 23-36 | 14 | |
| α-helix | 45-54 | 10 | |
| α-helix | 62-71 | 10 | |
| β-strand | 86-90 | 5 | 1 |
| α-helix | 94-105 | 12 | |
| β-strand | 109-114 | 6 | 1 |
| β-strand | 124-126 | 3 | 2 |
| α-helix | 129-137 | 9 | |
| α-helix | 140-143 | 4 | |
| β-strand | 154-156 | 3 | 2 |
| α-helix | 157-171 | 15 | |
| β-strand | 174-177 | 4 | 1 |
| β-strand | 180-185 | 6 | 3 |
| β-strand | 194 | 1 | 4 |
| β-strand | 195-199 | 5 | 3 |
| α-helix | 201-203 | 3 | |
| α-helix | 204-207 | 4 | |
| β-strand | 211 | 1 | 4 |
| β-strand | 213-216 | 4 | 1 |
| β-strand | 229-232 | 4 | 5 |
| β-strand | 238-245 | 8 | 6 |
| α-helix | 250-253 | 4 | |
| α-helix | 255-257 | 3 | |
| β-strand | 259-261 | 3 | 6 |
| β-strand | 265 | 1 | 6 |
| α-helix | 267-276 | 10 | |
| β-strand | 281-288 | 8 | 6 |
| β-strand | 291-298 | 8 | 6 |
| α-helix | 300-306 | 7 | |
| β-strand | 309 | 1 | 7 |
| α-helix | 316-319 | 4 | |
| β-strand | 325 | 1 | 7 |
| α-helix | 327-341 | 15 | |
| β-strand | 351 | 1 | 6 |
| α-helix | 352 | 1 | |
| β-strand | 353 | 1 | 8 |
| β-strand | 359 | 1 | 8 |
| β-strand | 361-365 | 5 | 6 |
| β-strand | 369-372 | 4 | 5 |
| β-strand | 376-381 | 6 | 1 |
| β-strand | 384-390 | 7 | 1 |
| α-helix | 392-394 | 3 | |
| β-strand | 396 | 1 | 5 |
| α-helix | 397-399 | 3 | |
| α-helix | 400-402 | 3 | |
| α-helix | 405-424 | 20 | |
| α-helix | 429-440 | 12 | |
| α-helix | 443-445 | 3 | |
| α-helix | 455-457 | 3 | |
| α-helix | 462-464 | 3 | |
| α-helix | 476-482 | 7 | |
| β-strand | 483-485 | 3 | 1 |
| α-helix | 510-522 | 13 | |
| α-helix | 541-550 | 10 | |
| α-helix | 557-561 | 5 | |
| α-helix | 567-575 | 9 | |
| α-helix | 576-580 | 5 | |
| α-helix | 588-593 | 6 | |
| α-helix | 597-610 | 14 | |
| α-helix | 631-644 | 14 | |
| α-helix | 703-704 | 2 | |
| β-strand | 709-712 | 4 | 9 |
| β-strand | 715-718 | 4 | 9 |
| β-strand | 723 | 1 | 10 |
| α-helix | 729 | 1 | |
| β-strand | 730 | 1 | 10 |
| α-helix | 731 | 1 | |
| β-strand | 736-739 | 4 | 11 |
| β-strand | 744-747 | 4 | 11 |
| α-helix | 909-958 | 50 | |
| α-helix | 964-1014 | 51 | |
| α-helix | 1024-1060 | 37 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| [F-actin]-monooxygenase MICAL1 | A | protein | 1067 | Homo sapiens | Q8TDZ2 (AlphaFold model) |
>9EWY_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
Structural basis of MICAL autoinhibition. Horvath, M., Schrofel, A., Kowalska, K. et al. Nat Commun (2024) 15:9810-9810. DOI 10.1038/s41467-024-54131-2 · 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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