Research workbench
Crystal structure of FEPYR1 in complex with abscisic acid
Analyse Crystal structure of FEPYR1 in complex with abscisic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UJV
- Type
- protein
- Length
- 574 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PYR1
- UniProt
- A0A2D1UXN2
- Ligands
- A8S
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PYR1 | protein | 192 | 29% helix, 35% strand | A0A2D1UXN2 |
| B, C | PYR1 | protein | 191 | 29% helix, 34% strand | A0A2D1UXN2 |
Ligands and binding sites
- A8S · (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.81 | 0.93 | 31 | A8S |
| 2 | 265 | 0.76 | 0.88 | 26 | A8S |
| 3 | 245 | 0.70 | 0.85 | 25 | A8S |
| 4 | 604 | 0.68 | 0.77 | 55 | empty |
| 5 | 183 | 0.47 | 0.76 | 28 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1089 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 765 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 253 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5UJV · Crystal structure of FePYR1 in complex with abscisic acid · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A2D1UXN2
- Elsewhere: RCSB PDB 5UJV · PDBe 5UJV · UniProt A0A2D1UXN2
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