MolNFT v1 · #119907 · protein
Crystal structure of arabidopsis thaliana ACO2 in complex with poa
5GJ9 · 1-aminocyclopropane-1-carboxylate oxidase 2: “Crystal structure of arabidopsis thaliana ACO2 in complex with poa”. X-ray diffraction, 2 ligands (VGL, ZN), 4 pockets (best druggability 0.69). MolNFT v1 #119907 on GenesisL1: 3D…
- PDB
- 5GJ9
- Type
- protein
- Length
- 596 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1-aminocyclopropane-1-carboxylate oxidase 2
- EC
- 1.14.17.4
- UniProt
- Q41931
- Ligands
- VGL, ZN
- Pockets
- 4 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 1-aminocyclopropane-1-carboxylate oxidase 2 (EC 1.14.17.4) | protein | 298 | 39% helix, 22% strand | Q41931 |
Ligands and binding sites
- VGL · Pyrazine-2-carboxylic acid · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 662 | 0.69 | 0.77 | 54 | empty |
| 2 | 270 | 0.65 | 0.82 | 42 | ZN, VGL |
| 3 | 220 | 0.65 | 0.83 | 37 | ZN, VGL |
| 4 | 53 | 0.26 | 0.73 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 339 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5GJ9 · Crystal structure of Arabidopsis thaliana ACO2 in complex with POA · the same entry in another collection · chain A against A, TM-score 1.00
- Q41931 · AlphaFold monomer V2.0 prediction for 1-aminocyclopropane-1-carboxylate oxidase 2 (Q41931) · 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 Q41931
- Elsewhere: RCSB PDB 5GJ9 · PDBe 5GJ9 · UniProt Q41931
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