The crystal structure of human Atg4B. Determined by X-ray diffraction at 1.9 Å resolution. Released 13 Sept 2005.
Explore 2CY7 in 3D Show helices and sheets RCSB PDB PDBe
2CY7 contains 20 α-helices and 18 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 | 10-13 | 4 | |
| α-helix | 18-20 | 3 | |
| β-strand | 26-28 | 3 | 1 |
| β-strand | 31-33 | 3 | 1 |
| α-helix | 39-48 | 10 | |
| β-strand | 50 | 1 | 2 |
| β-strand | 54-56 | 3 | 3 |
| α-helix | 58-60 | 3 | |
| β-strand | 68 | 1 | 3 |
| α-helix | 74-91 | 18 | |
| α-helix | 103-105 | 3 | |
| α-helix | 106-113 | 8 | |
| α-helix | 125-133 | 9 | |
| α-helix | 141-144 | 4 | |
| α-helix | 145-156 | 12 | |
| β-strand | 165-168 | 4 | 1 |
| β-strand | 173-175 | 3 | 4 |
| α-helix | 176-183 | 8 | |
| β-strand | 184 | 1 | 5 |
| β-strand | 219 | 1 | 5 |
| α-helix | 220-221 | 2 | |
| β-strand | 222-229 | 8 | 1 |
| α-helix | 237-239 | 3 | |
| α-helix | 240-246 | 7 | |
| β-strand | 252-257 | 6 | 1 |
| β-strand | 264-270 | 7 | 1 |
| β-strand | 273-277 | 5 | 1 |
| β-strand | 282-284 | 3 | 3 |
| α-helix | 285-286 | 2 | |
| α-helix | 297-299 | 3 | |
| β-strand | 300 | 1 | 2 |
| α-helix | 304-305 | 2 | |
| β-strand | 306-309 | 4 | 1 |
| α-helix | 310-312 | 3 | |
| β-strand | 316-323 | 8 | 1 |
| α-helix | 326-341 | 16 | |
| β-strand | 350-352 | 3 | 4 |
| α-helix | 371-376 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cysteine protease APG4B | A | protein | 396 | Homo sapiens | Q9Y4P1 (AlphaFold model) |
>2CY7_1 Cysteine protease APG4B (chains A) GPHMDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRKN FPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFID RKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVME EIRRLCRTSVPCAGATAFPADSDRHCNGFPAGAEVTNRPSPWRPLVLLIPLRLGLTDINE AYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEPTDGCFIPDE SFHCQHPPCRMSIAELDPSIAVGFFCKTEDDFNDWCQQVKKLSLLGGALPMFELVEQQPS HLACPDVLNLSLDSSDVERLERFFDSEDEDFEILSL
Structural Basis for the Specificity and Catalysis of Human Atg4B Responsible for Mammalian Autophagy. Sugawara, K., Suzuki, N.N., Fujioka, Y. et al. J Biol Chem (2005) 280:40058-40065. DOI 10.1074/jbc.M509158200 · PubMed
Other PDB entries of the same protein (UniProt Q9Y4P1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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