Research workbench
Crystal structures of PYR1/HAB1 in complex with synthetic analogues of abscisic acid
Analyse Crystal structures of PYR1/HAB1 in complex with synthetic analogues of abscisic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OR2
- Type
- protein
- Length
- 474 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O49686, Q9CAJ0
- Ligands
- A4H, MN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 179 | — | O49686 |
| B | — | protein | 295 | — | Q9CAJ0 |
Ligands and binding sites
- A4H · (2~{Z},4~{E})-3-cyclopropyl-5-[(1~{S})-2,6,6-trimethyl-1-oxidanyl-4-oxidanylidene-cyclohex-2-en-1-yl]penta-2, 4-dienoic acid · ligand · chains A
- MN · Manganese (II) ion · metal · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- Q9CAJ0 · AlphaFold monomer V2.0 prediction for protein phosphatase 2C 16 (Q9CAJ0) · a predicted model of the same protein · chain B against A, TM-score 0.99
- O49686 · AlphaFold monomer V2.0 prediction for abscisic acid receptor PYR1 (O49686) · a predicted model of the same protein · chain A 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 O49686
- Every structure of UniProt Q9CAJ0
- Elsewhere: RCSB PDB 5OR2 · PDBe 5OR2 · UniProt O49686 · UniProt Q9CAJ0
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