Research workbench
High-resolution structure of native malus domestica acc synthase
Analyse High-resolution structure of native malus domestica acc synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PIU
- Type
- protein
- Length
- 409 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-aminocyclopropane-1-carboxylate synthase
- EC
- 4.4.1.14
- UniProt
- P37821
- Ligands
- PLR
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) | protein | 409 | 48% helix, 16% strand | P37821 |
Ligands and binding sites
- PLR · (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 86 | 0.63 | 0.90 | 28 | empty |
| 2 | 225 | 0.52 | 0.76 | 27 | empty |
| 3 | 59 | 0.30 | 0.75 | 13 | empty |
| 4 | 51 | 0.26 | 0.74 | 19 | empty |
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, cofactor).
Compared structures
- 3PIU · High-resolution structure of native Malus domestica ACC synthase · the same entry in another collection · chain A against A, TM-score 1.00
- P37821 · AlphaFold monomer V2.0 prediction for 1-aminocyclopropane-1-carboxylate synthase (P37821) · a predicted model of the same protein · 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 P37821
- Elsewhere: RCSB PDB 3PIU · PDBe 3PIU · UniProt P37821
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