Research workbench
Structure of the GGA1-appendage in complex with the P56 binding peptide
Analyse Structure of the GGA1-appendage in complex with the P56 binding peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OM9
- Type
- protein
- Length
- 305 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor binding protein GGA1; 15-mer peptide fragment of P56
- UniProt
- Q9UJY5
- Pockets
- 4 · best druggability 0.53
Structure
x-ray diffraction · 3 distinct chains · 2% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ADP-ribosylation factor binding protein GGA1 | protein | 142 | 2% helix, 47% strand | Q9UJY5 |
| P | 15-mer peptide fragment of P56 | protein | 11 | 0% helix, 18% strand | — |
| Q | 15-mer peptide fragment of P56 | protein | 10 | 0% helix, 20% strand | — |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.53 | 0.87 | 22 | empty |
| 2 | 51 | 0.51 | 0.87 | 19 | empty |
| 3 | 84 | 0.44 | 0.80 | 15 | empty |
| 4 | 53 | 0.32 | 0.77 | 12 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1241 Ų buried · 4 hydrogen bonds · protein-protein
- A–P · 645 Ų buried · 5 hydrogen bonds · protein-protein
- B–Q · 588 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1OM9 · Structure of the GGA1-appendage in complex with the p56 binding peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UJY5 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-binding protein GGA1… · a predicted model of the same protein · chain B against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9UJY5
- Elsewhere: RCSB PDB 1OM9 · PDBe 1OM9 · UniProt Q9UJY5
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