MolNFT v1 · #115016 · protein
ATP-driven lipid-linked oligosaccharide flippase pglk in outward- occluded conformation
5C73 · Protein glycosylation K: “ATP-driven lipid-linked oligosaccharide flippase pglk in outward- occluded conformation”. X-ray diffraction, 20 pockets (best druggability 0.79). MolNFT v1 #115016 on GenesisL1: 3D structure, binding sites…
- PDB
- 5C73
- Type
- protein
- Length
- 3,384 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein glycosylation K
- EC
- 3.6.3.39
- UniProt
- Q0P9C4
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, K, A, B, G, F | Protein glycosylation K (EC 3.6.3.39) | protein | 564 | 49% helix, 5% strand | Q0P9C4 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.79 | 0.84 | 81 | empty |
| 2 | 634 | 0.78 | 0.84 | 83 | empty |
| 3 | 637 | 0.78 | 0.84 | 75 | empty |
| 4 | 629 | 0.78 | 0.84 | 87 | empty |
| 5 | 634 | 0.78 | 0.84 | 80 | empty |
Interfaces
9 interfaces between chains.
- G–F · 2091 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 2007 Ų buried · 6 hydrogen bonds · protein-protein
- C–K · 1675 Ų buried · 4 hydrogen bonds · protein-protein
- B–G · 94 Ų buried · 0 hydrogen bonds · protein-protein
- C–A · 92 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- Q0P9C4 · AlphaFold monomer V2.0 prediction for protein glycosylation K (Q0P9C4) · a predicted model of the same protein · chain C against A, TM-score 0.84
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 Q0P9C4
- Elsewhere: RCSB PDB 5C73 · PDBe 5C73 · UniProt Q0P9C4
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