MolNFT v1 · #2205 · protein
Glycosyltransferase
1BPL · Alpha-1,4-glucan-4-glucanohydrolase: “Glycosyltransferase”. X-ray diffraction, 1 pocket (best druggability 0.56). MolNFT v1 #2205 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1BPL
- Type
- protein
- Length
- 469 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1,4-glucan-4-glucanohydrolase
- EC
- 3.2.1.1
- UniProt
- P06278
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1,4-glucan-4-glucanohydrolase (EC 3.2.1.1) | protein | 179 | 16% helix, 27% strand | P06278 |
| B | Alpha-1,4-glucan-4-glucanohydrolase (EC 3.2.1.1) | protein | 290 | 36% helix, 22% strand | P06278 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.56 | 0.75 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 3116 Ų buried · 56 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 P06278
- Elsewhere: RCSB PDB 1BPL · PDBe 1BPL · UniProt P06278
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