4NAW: Human ATG12~ATG5-ATG16N
Crystal Structure of Human ATG12~ATG5-ATG16N in complex with a fragment of ATG3. Determined by X-ray diffraction at 2.19 Å resolution. Released 6 Nov 2013.
- Method
- X-ray diffraction
- Resolution
- 2.19 Å
- Organism
- Homo sapiens
- Chains
- 16
- Atoms
- 13,933
- Mol. weight
- 206.15 kDa
- Released
- 6 Nov 2013
Explore 4NAW in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4NAW contains 90 α-helices and 97 β-strands across 16 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: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 55-61 | 7 | 1 |
| α-helix | 66-68 | 3 | |
| β-strand | 72-75 | 4 | 1 |
| β-strand | 80 | 1 | 2 |
| α-helix | 81-91 | 11 | |
| β-strand | 101-104 | 4 | 1 |
| β-strand | 108 | 1 | 1 |
| β-strand | 115 | 1 | 2 |
| α-helix | 116-123 | 8 | |
| β-strand | 125 | 1 | 1 |
| β-strand | 128-134 | 7 | 1 |
Chain B: 16 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-12 | 10 | |
| β-strand | 15-22 | 8 | 3 |
| α-helix | 31-34 | 4 | |
| β-strand | 35-40 | 6 | 3 |
| α-helix | 45-48 | 4 | |
| α-helix | 50-57 | 8 | |
| α-helix | 62-64 | 3 | |
| β-strand | 69-72 | 4 | 3 |
| β-strand | 75-76 | 2 | 3 |
| α-helix | 83-90 | 8 | |
| α-helix | 95 | 1 | |
| β-strand | 98-103 | 6 | 3 |
| 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 |
| α-helix | 272-273 | 2 | |
Chain C: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-25 | 14 | |
| α-helix | 26-30 | 5 | |
| α-helix | 31-42 | 12 | |
Chain D: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 155-156 | 2 | 1 |
| α-helix | 157-163 | 7 | |
Chain E: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 55-61 | 7 | 8 |
| α-helix | 66-68 | 3 | |
| β-strand | 72-75 | 4 | 8 |
| β-strand | 80 | 1 | 9 |
| α-helix | 81-91 | 11 | |
| α-helix | 99-100 | 2 | |
| β-strand | 101-104 | 4 | 8 |
| β-strand | 108 | 1 | 8 |
| β-strand | 115 | 1 | 9 |
| α-helix | 116-123 | 8 | |
| β-strand | 125 | 1 | 8 |
| β-strand | 128-134 | 7 | 8 |
Chain F: 16 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-12 | 8 | |
| β-strand | 15-22 | 8 | 10 |
| α-helix | 31-34 | 4 | |
| β-strand | 35-40 | 6 | 10 |
| α-helix | 45-48 | 4 | |
| α-helix | 50-57 | 8 | |
| α-helix | 62-64 | 3 | |
| β-strand | 69-72 | 4 | 10 |
| β-strand | 75-76 | 2 | 10 |
| α-helix | 77-78 | 2 | |
| α-helix | 83-90 | 8 | |
| α-helix | 95 | 1 | |
| β-strand | 98-103 | 6 | 10 |
| α-helix | 118-137 | 20 | |
| α-helix | 140-143 | 4 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| β-strand | 187-190 | 4 | 11 |
| β-strand | 199 | 1 | 11 |
| β-strand | 206 | 1 | 12 |
| α-helix | 211 | 1 | |
| β-strand | 212 | 1 | 12 |
| α-helix | 213 | 1 | |
| β-strand | 214 | 1 | 13 |
| α-helix | 215-222 | 8 | |
| β-strand | 236-239 | 4 | 11 |
| β-strand | 240 | 1 | 14 |
| β-strand | 243 | 1 | 14 |
| β-strand | 250 | 1 | 13 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-271 | 7 | 11 |
Chain G: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-28 | 17 | |
| α-helix | 33-42 | 10 | |
Chains H, L and P: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 155-156 | 2 | 8 |
| α-helix | 157-161 | 5 | |
6 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Ubiquitin-like protein ATG12 | A, E, I, M | protein | 91 | Homo sapiens | O94817 (AlphaFold model) |
| Autophagy protein 5 | B, F, J, N | protein | 275 | Homo sapiens | Q9H1Y0 (AlphaFold model) |
| Autophagy-related protein 16-1 | C, G, K, O | protein | 36 | Homo sapiens | Q676U5 (AlphaFold model) |
| Ubiquitin-like-conjugating enzyme ATG3 | D, H, L, P | protein | 34 | Homo sapiens | Q9NT62 (AlphaFold model) |
Sequence of entity 1 (A, E, I, M), FASTA
>4NAW_1 Ubiquitin-like protein ATG12 (chains A, E, I, M)
GSKKKIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFA
PSPDQEVGTLYECFGSDGKLVLHYCKSQAWG
Sequence of entity 2 (B, F, J, N), FASTA
>4NAW_2 Autophagy protein 5 (chains B, F, J, N)
MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKHFQKVM
RQEDISEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHCPSKDA
IEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLMEYPAEEN
GFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLKEVCPSAIDPEDGEKKNQVMI
HGIEPMLETPLQWLSEHLSYPDNFLHISIIPQPTD
Sequence of entity 3 (C, G, K, O), FASTA
>4NAW_3 Autophagy-related protein 16-1 (chains C, G, K, O)
SHMPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLL
Sequence of entity 4 (D, H, L, P), FASTA
>4NAW_4 Ubiquitin-like-conjugating enzyme ATG3 (chains D, H, L, P)
GHMSALCEEEEDEDEGEAADMEEYEESGLLETDE
Primary citation
Structural basis of ATG3 recognition by the autophagic ubiquitin-like protein ATG12. Metlagel, Z., Otomo, C., Takaesu, G. et al. Proc Natl Acad Sci U S A (2013) 110:18844-18849. DOI 10.1073/pnas.1314755110 · PubMed
Other PDB entries of the same protein (UniProt O94817 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 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…
Browse structure collections
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