8T31: GABARAP
Crystal structure of GABARAP in complex with the LIR of TP53INP2/DOR. Determined by X-ray diffraction at 2.1 Å resolution. Released 22 May 2024.
- Method
- X-ray diffraction
- Resolution
- 2.1 Å
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 5,370
- Mol. weight
- 78.51 kDa
- Released
- 22 May 2024
Explore 8T31 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8T31 contains 27 α-helices and 49 β-strands across 10 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 and G: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-8 | 5 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 1 |
| β-strand | 48-52 | 5 | 1 |
| β-strand | 56 | 1 | 2 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 1 |
| β-strand | 80 | 1 | 3 |
| β-strand | 83 | 1 | 3 |
| α-helix | 84-86 | 3 | |
| β-strand | 90 | 1 | 2 |
| α-helix | 91-98 | 8 | |
| β-strand | 105-110 | 6 | 1 |
Chain B: 1 helix, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 30-32 | 3 | 1 |
| β-strand | 35-37 | 3 | 1 |
| α-helix | 38-41 | 4 | |
Chain C: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-8 | 5 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 4 |
| β-strand | 48-52 | 5 | 4 |
| β-strand | 56 | 1 | 5 |
| α-helix | 57-67 | 11 | |
| β-strand | 77-79 | 3 | 4 |
| β-strand | 80 | 1 | 6 |
| β-strand | 83 | 1 | 6 |
| α-helix | 84-86 | 3 | |
| β-strand | 90 | 1 | 5 |
| α-helix | 91-98 | 8 | |
| β-strand | 105-110 | 6 | 4 |
Chain D: 0 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32 | 1 | 7 |
| β-strand | 35 | 1 | 7 |
| β-strand | 36-37 | 2 | 4 |
Chain E: 6 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-8 | 5 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 8 |
| α-helix | 42-43 | 2 | |
| β-strand | 48-52 | 5 | 8 |
| β-strand | 56 | 1 | 9 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 8 |
| β-strand | 80 | 1 | 10 |
| β-strand | 83 | 1 | 10 |
| α-helix | 84-86 | 3 | |
| β-strand | 90 | 1 | 9 |
| α-helix | 91-98 | 8 | |
| β-strand | 105-110 | 6 | 8 |
Chain F: 1 helix, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 31-32 | 2 | 8 |
| β-strand | 35-37 | 3 | 8 |
| α-helix | 38-40 | 3 | |
Chains H and J: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 36-37 | 2 | 11 |
Chain I: 4 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-8 | 5 | |
| α-helix | 11-24 | 14 | |
| β-strand | 28-35 | 8 | 14 |
| β-strand | 48-52 | 5 | 14 |
| β-strand | 56 | 1 | 15 |
| α-helix | 57-68 | 12 | |
| β-strand | 77-79 | 3 | 14 |
| β-strand | 80 | 1 | 16 |
| β-strand | 83 | 1 | 16 |
| β-strand | 90 | 1 | 15 |
| α-helix | 91-98 | 8 | |
| β-strand | 105-110 | 6 | 14 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Gamma-aminobutyric acid receptor-associated protein | A, C, E, G, I | protein | 119 | Homo sapiens | O95166 (AlphaFold model) |
| Tumor protein p53-inducible nuclear protein 2 | B, D, F, H, J | protein | 15 | Homo sapiens | Q8IXH6 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G, I), FASTA
>8T31_1 Gamma-aminobutyric acid receptor-associated protein (chains A, C, E, G, I)
GSMKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVG
QFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYGL
Sequence of entity 2 (B, D, F, H, J), FASTA
>8T31_2 Tumor protein p53-inducible nuclear protein 2 (chains B, D, F, H, J)
GSEVDGWLIIDLPDS
Primary citation
Structural and functional characterization of the role of acetylation on the interactions of the human Atg8-family proteins with the autophagy receptor TP53INP2/DOR. Ali, M.G., Wahba, H.M., Igelmann, S. et al. Autophagy (2024) 20:1948-1967. DOI 10.1080/15548627.2024.2353443 · PubMed
Other PDB entries of the same protein (UniProt O95166 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6HYO 1.07 Å, Structure of ULK1 LIR motif bound to GABARAP
- 6YOP 1.1 Å, Structure of SAMM50 LIR bound to GABARAP
- 7ZKR 1.1 Å, Human GABARAP in complex with stapled peptide Pen3-ortho
- 6HYN 1.14 Å, Structure of ATG13 LIR motif bound to GABARAP
- 7AA8 1.25 Å, Structure of SCOC LIR bound to GABARAP
- 6HOG 1.26 Å, Structure of VPS34 LIR motif bound to GABARAP
- 8T2M 1.27 Å, Crystal structure of GABARAP in complex with the LIR of NSs4
- 3D32 1.3 Å, Complex of GABA(A) receptor-associated protein (GABARAP) with a synthetic peptide
- 6HB9 1.3 Å, Crystal structure of the GABARAP in complex with the UBA5 LIR motif
- 7BRQ 1.4 Å, Crystal structure of human FAM134B LIR fused to human GABARAP
- 9I9X 1.42 Å, Human GABARAP in complex with artificial peptide IM-2
- 9HGD 1.5 Å, Crystal structure of human GABARAP in complex with cyclic peptide GAB_D23
Browse structure collections
About this viewer
MolViewer shows 8T31 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.