5JHC: Self-assembled propeptides from Ape1
Crystal structure of the self-assembled propeptides from Ape1. Determined by X-ray diffraction at 3.4 Å resolution. Released 29 Jun 2016.
- Method
- X-ray diffraction
- Resolution
- 3.4 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 39
- Atoms
- 6,607
- Mol. weight
- 111.55 kDa
- Released
- 29 Jun 2016
Explore 5JHC in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5JHC contains 39 α-helices and 0 β-strands across 39 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.
Chains a, A, b, H, i, j, L, P and R: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 1-21 | 21 | |
Chains B, c, C, e, E, F, g, G, h, I, J, k, K, l, M, N, Q, T, V and X: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-21 | 22 | |
Chains d, f and O: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-20 | 21 | |
Chains D, m and S: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-21 | 20 | |
Chain U: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-19 | 20 | |
Chain W: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-18 | 19 | |
Chain Y: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-16 | 17 | |
Chain Z: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 0-11 | 12 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Vacuolar aminopeptidase 1 | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, j, k, l, m | protein | 24 | Saccharomyces cerevisiae | P14904 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, j, k, l, m), FASTA
>5JHC_1 Vacuolar aminopeptidase 1 (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, d, e, f, g, h, i, j, k, l, m)
GPMEEQREILEQLKKTLQMLTVEL
Primary citation
Structural Basis for Receptor-Mediated Selective Autophagy of Aminopeptidase I Aggregates. Yamasaki, A., Watanabe, Y., Adachi, W. et al. Cell Rep (2016) 16:19-27. DOI 10.1016/j.celrep.2016.05.066 · PubMed
Other PDB entries of the same protein (UniProt P14904 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5JGF 1.83 Å, Crystal structure of mApe1
- 5JGE 1.91 Å, Crystal structure of Atg19 coiled-coil complexed with Ape1 propeptide
- 5JH9 2.1 Å, Crystal structure of prApe1
- 4R8F 2.5 Å, Crystal structure of yeast aminopeptidase 1 (Ape1)
- 5JM9 24.0 Å, Structure of S. cerevesiae mApe1 dodecamer
Browse structure collections
About this viewer
MolViewer shows 5JHC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.