MolNFT v1 · #115641 · protein
Disproportionating enzyme 1 from arabidopsis - apo form
5CPQ · 4-alpha-glucanotransferase DPE1, CHLOROPLASTIC/AMYLOPLASTIC: “Disproportionating enzyme 1 from arabidopsis - apo form”. X-ray diffraction, 8 pockets (best druggability 0.77). MolNFT v1 #115641 on GenesisL1: 3D structure, binding…
- PDB
- 5CPQ
- Type
- protein
- Length
- 1,026 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-alpha-glucanotransferase DPE1, CHLOROPLASTIC/AMYLOPLASTIC
- EC
- 2.4.1.25
- UniProt
- Q9LV91
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-alpha-glucanotransferase DPE1, CHLOROPLASTIC/AMYLOPLASTIC (EC 2.4.1.25) | protein | 512 | 47% helix, 12% strand | Q9LV91 |
| B | 4-alpha-glucanotransferase DPE1, CHLOROPLASTIC/AMYLOPLASTIC (EC 2.4.1.25) | protein | 514 | 47% helix, 12% strand | Q9LV91 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 14 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 308 | 0.77 | 0.88 | 31 | empty |
| 2 | 1039 | 0.75 | 0.78 | 107 | EDO |
| 3 | 504 | 0.68 | 0.79 | 64 | EDO |
| 4 | 311 | 0.63 | 0.80 | 31 | EDO |
| 5 | 410 | 0.58 | 0.75 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 2057 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
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 Q9LV91
- Elsewhere: RCSB PDB 5CPQ · PDBe 5CPQ · UniProt Q9LV91
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