5D7G: Human ATG5 E122D-ATG16L1 complex
Structure of human ATG5 E122D-ATG16L1 complex at 3.0 Angstroms. Determined by X-ray diffraction at 3.0 Å resolution. Released 3 Feb 2016.
- Method
- X-ray diffraction
- Resolution
- 3.0 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 9,417
- Mol. weight
- 165.49 kDa
- Released
- 3 Feb 2016
Explore 5D7G in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5D7G contains 68 α-helices and 64 β-strands across 8 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: 14 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-12 | 8 | |
| β-strand | 15-22 | 8 | 1 |
| β-strand | 28 | 1 | 2 |
| α-helix | 33-34 | 2 | |
| β-strand | 35-40 | 6 | 1 |
| β-strand | 44 | 1 | 3 |
| α-helix | 50-59 | 10 | |
| β-strand | 60 | 1 | 2 |
| β-strand | 69-72 | 4 | 1 |
| β-strand | 75-76 | 2 | 1 |
| α-helix | 77 | 1 | |
| β-strand | 82 | 1 | 3 |
| α-helix | 83-90 | 8 | |
| α-helix | 95 | 1 | |
| β-strand | 98-103 | 6 | 1 |
| α-helix | 118-137 | 20 | |
| α-helix | 140-144 | 5 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| β-strand | 187-190 | 4 | 4 |
| β-strand | 199 | 1 | 4 |
| β-strand | 206 | 1 | 5 |
| α-helix | 211 | 1 | |
| β-strand | 212 | 1 | 5 |
| α-helix | 213 | 1 | |
| β-strand | 214 | 1 | 6 |
| α-helix | 215-222 | 8 | |
| β-strand | 236-239 | 4 | 4 |
| β-strand | 240 | 1 | 7 |
| β-strand | 243 | 1 | 7 |
| β-strand | 250 | 1 | 6 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-271 | 7 | 4 |
Chain B: 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 C: 16 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-12 | 8 | |
| β-strand | 15-22 | 8 | 8 |
| α-helix | 23 | 1 | |
| α-helix | 33-34 | 2 | |
| β-strand | 35-40 | 6 | 8 |
| β-strand | 44 | 1 | 9 |
| α-helix | 50-57 | 8 | |
| β-strand | 69-72 | 4 | 8 |
| β-strand | 75-76 | 2 | 8 |
| α-helix | 77-78 | 2 | |
| β-strand | 82 | 1 | 9 |
| α-helix | 83-90 | 8 | |
| α-helix | 95 | 1 | |
| β-strand | 98-103 | 6 | 8 |
| α-helix | 118-137 | 20 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| α-helix | 177-179 | 3 | |
| β-strand | 187-190 | 4 | 10 |
| α-helix | 197-198 | 2 | |
| β-strand | 199 | 1 | 10 |
| β-strand | 206 | 1 | 11 |
| α-helix | 211 | 1 | |
| β-strand | 212 | 1 | 11 |
| α-helix | 213 | 1 | |
| β-strand | 214 | 1 | 12 |
| α-helix | 215-222 | 8 | |
| β-strand | 236-239 | 4 | 10 |
| β-strand | 240 | 1 | 13 |
| β-strand | 243 | 1 | 13 |
| β-strand | 250 | 1 | 12 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-271 | 7 | 10 |
Chain D: 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 E: 14 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-12 | 8 | |
| β-strand | 15-22 | 8 | 14 |
| β-strand | 35-40 | 6 | 14 |
| α-helix | 50-58 | 9 | |
| β-strand | 69-72 | 4 | 14 |
| β-strand | 75-76 | 2 | 14 |
| α-helix | 83-90 | 8 | |
| α-helix | 95 | 1 | |
| β-strand | 98-103 | 6 | 14 |
| α-helix | 118-137 | 20 | |
| α-helix | 140-144 | 5 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| β-strand | 187-191 | 5 | 15 |
| α-helix | 197-198 | 2 | |
| β-strand | 199 | 1 | 15 |
| β-strand | 206 | 1 | 16 |
| α-helix | 211 | 1 | |
| β-strand | 212 | 1 | 16 |
| α-helix | 213 | 1 | |
| β-strand | 214 | 1 | 17 |
| α-helix | 215-222 | 8 | |
| β-strand | 236-239 | 4 | 15 |
| β-strand | 240 | 1 | 18 |
| β-strand | 243 | 1 | 18 |
| β-strand | 250 | 1 | 17 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-271 | 7 | 15 |
| α-helix | 272-273 | 2 | |
Chain F: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-25 | 14 | |
| α-helix | 26-30 | 5 | |
| α-helix | 31-48 | 18 | |
Chain G: 12 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-13 | 9 | |
| β-strand | 15-22 | 8 | 19 |
| α-helix | 23 | 1 | |
| α-helix | 31-34 | 4 | |
| β-strand | 35-40 | 6 | 19 |
| α-helix | 45-48 | 4 | |
| α-helix | 50-59 | 10 | |
| β-strand | 69-72 | 4 | 19 |
| β-strand | 75-76 | 2 | 19 |
| α-helix | 83-90 | 8 | |
| α-helix | 95 | 1 | |
| β-strand | 98-103 | 6 | 19 |
| α-helix | 118-137 | 20 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| β-strand | 187-191 | 5 | 20 |
| β-strand | 199 | 1 | 20 |
| β-strand | 214 | 1 | 21 |
| α-helix | 215-222 | 8 | |
| β-strand | 237-239 | 3 | 20 |
| β-strand | 240 | 1 | 22 |
| β-strand | 243 | 1 | 22 |
| β-strand | 250 | 1 | 21 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-270 | 6 | 20 |
Chain H: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-24 | 13 | |
| α-helix | 25-30 | 6 | |
| α-helix | 31-47 | 17 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Autophagy protein 5 | A, C, E, G | protein | 280 | Homo sapiens | Q9H1Y0 (AlphaFold model) |
| Autophagy-related protein 16-1 | B, D, F, H | protein | 71 | Homo sapiens | Q676U5 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G), FASTA
>5D7G_1 Autophagy protein 5 (chains A, C, E, G)
GAMGSMTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKH
FQKVMRQEDISEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHC
PSKDAIDAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLMEY
PAEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLKEVCPSAIDPEDGEKK
NQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIIPQPTD
Sequence of entity 2 (B, D, F, H), FASTA
>5D7G_2 Autophagy-related protein 16-1 (chains B, D, F, H)
GSMSSGLRAADFPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQA
EKHDVPNRHEI
Primary citation
Mutation in ATG5 reduces autophagy and leads to ataxia with developmental delay. Kim, M., Sandford, E., Gatica, D. et al. Elife (2016) 5. DOI 10.7554/eLife.12245 · 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
- 4TQ0 2.7 Å, Crystal structure of human ATG5-ATG16N69
- 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…
- 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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