Structure of human Atg4b. Determined by X-ray diffraction at 2.0 Å resolution. Released 10 Jan 2006.
Explore 2D1I in 3D Show helices and sheets RCSB PDB PDBe
2D1I contains 38 α-helices and 34 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 | 11-13 | 3 | |
| α-helix | 25 | 1 | |
| β-strand | 26-28 | 3 | 1 |
| β-strand | 31-33 | 3 | 1 |
| α-helix | 39-48 | 10 | |
| β-strand | 50 | 1 | 2 |
| α-helix | 51 | 1 | |
| β-strand | 54-56 | 3 | 3 |
| α-helix | 58-60 | 3 | |
| α-helix | 61-63 | 3 | |
| α-helix | 74-91 | 18 | |
| α-helix | 103-105 | 3 | |
| α-helix | 106-113 | 8 | |
| α-helix | 125-133 | 9 | |
| α-helix | 142-144 | 3 | |
| 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 | 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 | 326-339 | 14 | |
| β-strand | 350-352 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-13 | 3 | |
| α-helix | 25 | 1 | |
| β-strand | 26-28 | 3 | 6 |
| β-strand | 31-33 | 3 | 6 |
| α-helix | 39-48 | 10 | |
| β-strand | 50 | 1 | 7 |
| β-strand | 55-56 | 2 | 8 |
| α-helix | 58-60 | 3 | |
| α-helix | 74-91 | 18 | |
| α-helix | 103-105 | 3 | |
| α-helix | 106-113 | 8 | |
| α-helix | 125-133 | 9 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-156 | 12 | |
| β-strand | 165-168 | 4 | 6 |
| β-strand | 173-175 | 3 | 9 |
| α-helix | 176-183 | 8 | |
| β-strand | 184 | 1 | 10 |
| β-strand | 219 | 1 | 10 |
| β-strand | 222-229 | 8 | 6 |
| α-helix | 237-239 | 3 | |
| α-helix | 240-246 | 7 | |
| β-strand | 252-257 | 6 | 6 |
| β-strand | 264-270 | 7 | 6 |
| β-strand | 273-277 | 5 | 6 |
| β-strand | 283-284 | 2 | 8 |
| α-helix | 285-287 | 3 | |
| α-helix | 297-299 | 3 | |
| β-strand | 300 | 1 | 7 |
| α-helix | 304-305 | 2 | |
| β-strand | 306-309 | 4 | 6 |
| α-helix | 310-312 | 3 | |
| β-strand | 316-323 | 8 | 6 |
| α-helix | 326-338 | 13 | |
| β-strand | 350-352 | 3 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cysteine protease APG4B | A, B | protein | 398 | Homo sapiens | Q9Y4P1 (AlphaFold model) |
>2D1I_1 Cysteine protease APG4B (chains A, B) GPLGSMDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYR KNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAF IDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVV MEEIRRLCRTSVPCAGATAFPADSDRHCNGFPAGAEVTNRPSPWRPLVLLIPLRLGLTDI NEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEPTDGCFIP DESFHCQHPPCRMSIAELDPSIAVGFFCKTEDDFNDWCQQVKKLSLLGGALPMFELVEQQ PSHLACPDVLNLSLDSSDVERLERFFDSEDEDFEILSL
The Crystal Structure of Human Atg4b, a Processing and De-conjugating Enzyme for Autophagosome-forming Modifiers. Kumanomidou, T., Mizushima, T., Komatsu, M. et al. J Mol Biol (2006) 355:612-618. DOI 10.1016/j.jmb.2005.11.018 · 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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