MolNFT v1 · #36335 · protein
X-ray structure of gene product from arabidopsis thaliana AT3G16990
2F2G · Seed maturation protein PM36 homolog: “X-ray structure of gene product from arabidopsis thaliana AT3G16990”. X-ray diffraction, 2 ligands (HMH, SO4), 3 pockets (best druggability 0.60). MolNFT v1 #36335 on GenesisL1: 3D structure…
- PDB
- 2F2G
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Seed maturation protein PM36 homolog
- UniProt
- Q9ASY9
- Ligands
- HMH, SO4
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Seed maturation protein PM36 homolog | protein | 215 | 73% helix, 3% strand | Q9ASY9 |
| B | Seed maturation protein PM36 homolog | protein | 211 | 80% helix, 0% strand | Q9ASY9 |
Ligands and binding sites
- HMH · 4-amino-5-hydroxymethyl-2-methylpyrimidine · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.60 | 0.84 | 21 | empty |
| 2 | 64 | 0.33 | 0.76 | 14 | empty |
| 3 | 59 | 0.32 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 8 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 2F2G · X-Ray Structure of Gene Product From Arabidopsis Thaliana AT3G16990 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ASY9 · AlphaFold monomer V2.0 prediction for bifunctional tena-E protein (Q9ASY9) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9ASY9
- Elsewhere: RCSB PDB 2F2G · PDBe 2F2G · UniProt Q9ASY9
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