4TQ0: Human ATG5-ATG16N69
Crystal structure of human ATG5-ATG16N69. Determined by X-ray diffraction at 2.7 Å resolution. Released 11 Mar 2015.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 7,219
- Mol. weight
- 127.17 kDa
- Released
- 11 Mar 2015
Explore 4TQ0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4TQ0 contains 57 α-helices and 45 β-strands across 6 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.
Chain A: 18 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-12 | 8 | |
| β-strand | 15-22 | 8 | 1 |
| β-strand | 35-40 | 6 | 1 |
| α-helix | 45-48 | 4 | |
| α-helix | 50-55 | 6 | |
| β-strand | 68-72 | 5 | 1 |
| β-strand | 75-76 | 2 | 1 |
| α-helix | 77-78 | 2 | |
| α-helix | 83-86 | 4 | |
| α-helix | 87-91 | 5 | |
| α-helix | 95 | 1 | |
| β-strand | 98-104 | 7 | 1 |
| α-helix | 118-136 | 19 | |
| α-helix | 141-144 | 4 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| α-helix | 177-179 | 3 | |
| β-strand | 187-191 | 5 | 2 |
| α-helix | 197-198 | 2 | |
| β-strand | 199 | 1 | 2 |
| β-strand | 206 | 1 | 3 |
| α-helix | 211 | 1 | |
| β-strand | 212 | 1 | 3 |
| α-helix | 213 | 1 | |
| β-strand | 214 | 1 | 4 |
| α-helix | 215-222 | 8 | |
| α-helix | 224-226 | 3 | |
| β-strand | 236-239 | 4 | 2 |
| β-strand | 240 | 1 | 5 |
| β-strand | 243 | 1 | 5 |
| β-strand | 250 | 1 | 4 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-271 | 7 | 2 |
Chain B: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-25 | 14 | |
| α-helix | 26-30 | 5 | |
| α-helix | 31-47 | 17 | |
Chain C: 18 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-13 | 9 | |
| β-strand | 15-22 | 8 | 6 |
| β-strand | 35-40 | 6 | 6 |
| α-helix | 45-48 | 4 | |
| α-helix | 50-57 | 8 | |
| β-strand | 68-72 | 5 | 6 |
| β-strand | 75-76 | 2 | 6 |
| α-helix | 77-78 | 2 | |
| α-helix | 83-86 | 4 | |
| α-helix | 87-91 | 5 | |
| α-helix | 95 | 1 | |
| β-strand | 98-104 | 7 | 6 |
| α-helix | 118-136 | 19 | |
| α-helix | 141-144 | 4 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| α-helix | 177-179 | 3 | |
| β-strand | 187-191 | 5 | 7 |
| α-helix | 197-198 | 2 | |
| β-strand | 199 | 1 | 7 |
| β-strand | 206 | 1 | 8 |
| α-helix | 211 | 1 | |
| β-strand | 212 | 1 | 8 |
| α-helix | 213 | 1 | |
| β-strand | 214 | 1 | 9 |
| α-helix | 215-222 | 8 | |
| α-helix | 224-226 | 3 | |
| β-strand | 236-239 | 4 | 7 |
| β-strand | 240 | 1 | 10 |
| β-strand | 243 | 1 | 10 |
| β-strand | 250 | 1 | 9 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-271 | 7 | 7 |
Chain D: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-25 | 14 | |
| α-helix | 26-30 | 5 | |
| α-helix | 31-45 | 15 | |
Chain E: 14 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-13 | 9 | |
| β-strand | 15-22 | 8 | 11 |
| α-helix | 31-34 | 4 | |
| β-strand | 35-40 | 6 | 11 |
| α-helix | 45-48 | 4 | |
| α-helix | 50-57 | 8 | |
| β-strand | 70-72 | 3 | 11 |
| β-strand | 75-76 | 2 | 11 |
| α-helix | 77-78 | 2 | |
| α-helix | 83-90 | 8 | |
| α-helix | 95 | 1 | |
| β-strand | 98-102 | 5 | 11 |
| α-helix | 118-136 | 19 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| β-strand | 187-191 | 5 | 12 |
| α-helix | 197-198 | 2 | |
| β-strand | 199 | 1 | 12 |
| β-strand | 206-207 | 2 | 13 |
| β-strand | 211-212 | 2 | 13 |
| α-helix | 213 | 1 | |
| β-strand | 214 | 1 | 14 |
| α-helix | 215-222 | 8 | |
| β-strand | 236-239 | 4 | 12 |
| β-strand | 240 | 1 | 15 |
| β-strand | 243 | 1 | 15 |
| β-strand | 250 | 1 | 14 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-271 | 7 | 12 |
Chain F: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-46 | 35 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Autophagy protein 5 | A, C, E | protein | 289 | Homo sapiens | Q9H1Y0 (AlphaFold model) |
| Autophagy-related protein 16-1 | B, D, F | protein | 69 | Homo sapiens | Q676U5 (AlphaFold model) |
Sequence of entity 1 (A, C, E), FASTA
>4TQ0_1 Autophagy protein 5 (chains A, C, E)
MGSSHHHHHHSQGSMTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLT
LVTDKVKKHFQKVMRQEDISEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKS
FPEKDLLHCPSKDAIEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFW
AINRKLMEYPAEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLKEVCPSA
IDPEDGEKKNQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIIPQPTD
Sequence of entity 2 (B, D, F), FASTA
>4TQ0_2 Autophagy-related protein 16-1 (chains B, D, F)
MSSGLRAADFPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQAEK
HDVPNRHEI
Primary citation
Insights into autophagosome maturation revealed by the structures of ATG5 with its interacting partners. Kim, J.H., Hong, S.B., Lee, J.K. et al. Autophagy (2015) 11:75-87. DOI 10.4161/15548627.2014.984276 · PubMed
Other PDB entries of the same protein (UniProt Q9H1Y0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4TQ1 1.8 Å, Crystal structure of human ATG5-TECAIR
- 4NAW 2.19 Å, Crystal Structure of Human ATG12~ATG5-ATG16N in complex with a fragment of ATG3
- 4GDK 2.7 Å, Crystal Structure of Human Atg12~Atg5 Conjugate in Complex with an N-terminal Fragment…
- 4GDL 2.88 Å, Crystal Structure of Human Atg12~Atg5 Conjugate in Complex with an N-terminal Fragment…
- 5D7G 3.0 Å, Structure of human ATG5 E122D-ATG16L1 complex at 3.0 Angstroms
- 7W36 3.0 Å, Crystal structure of human Atg5 complexed with a stapled peptide
- 5NPV 3.1 Å, Structure of human ATG5-ATG16L1(ATG5BD) complex (I4)
- 5NPW 3.1 Å, Structure of human ATG5-ATG16L1(ATG5BD) complex (C2)
Browse structure collections
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