Structure of human ATG5-ATG16L1(ATG5BD) complex (I4). Determined by X-ray diffraction at 3.1 Å resolution. Released 11 Oct 2017.
Explore 5NPV in 3D Show helices and sheets RCSB PDB PDBe
5NPV contains 35 α-helices and 29 β-strands across 4 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 | 5-12 | 8 | |
| β-strand | 15-22 | 8 | 1 |
| β-strand | 35-40 | 6 | 1 |
| α-helix | 45-57 | 13 | |
| β-strand | 69-72 | 4 | 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 | 98-103 | 6 | 1 |
| α-helix | 118-136 | 19 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-169 | 8 | |
| α-helix | 171-173 | 3 | |
| β-strand | 187-191 | 5 | 2 |
| β-strand | 198-199 | 2 | 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 | 215-221 | 7 | |
| α-helix | 224-226 | 3 | |
| β-strand | 237-239 | 3 | 2 |
| β-strand | 240 | 1 | 5 |
| β-strand | 243 | 1 | 5 |
| β-strand | 250 | 1 | 4 |
| α-helix | 251-253 | 3 | |
| α-helix | 254-258 | 5 | |
| β-strand | 265-270 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-28 | 17 | |
| α-helix | 30-45 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-12 | 8 | |
| β-strand | 15-21 | 7 | 6 |
| β-strand | 35-40 | 6 | 6 |
| α-helix | 45-53 | 9 | |
| β-strand | 68-71 | 4 | 6 |
| β-strand | 76 | 1 | 6 |
| α-helix | 77 | 1 | |
| 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 | 140-144 | 5 | |
| α-helix | 147-158 | 12 | |
| α-helix | 162-172 | 11 | |
| β-strand | 188-191 | 4 | 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 | |
| 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 | 266-271 | 6 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-24 | 13 | |
| α-helix | 25-29 | 5 | |
| α-helix | 30-46 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Autophagy protein 5 | A, C | protein | 282 | Homo sapiens | Q9H1Y0 (AlphaFold model) |
| Autophagy-related protein 16-1 | B, D | protein | 301 | Homo sapiens | Q676U5 (AlphaFold model) |
>5NPV_1 Autophagy protein 5 (chains A, C) GAHMSGRMTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVK KHFQKVMRQEDISEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLL HCPSKDAIEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLM EYPAEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLKEVCPSAIDPEDGE KKNQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIIPQPTD
>5NPV_2 Autophagy-related protein 16-1 (chains B, D) GGGRPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNR HEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQM NEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEE NQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDE TSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGK E
Identification, biochemical characterization and crystallization of the central region of human ATG16L1. Archna, A., Scrima, A. Acta Crystallogr F Struct Biol Commun (2017) 73:560-567. DOI 10.1107/S2053230X17013280 · PubMed
Other PDB entries of the same protein (UniProt Q9H1Y0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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