MolNFT v1 · #160277 · protein
Structure of kluyveromyces marxianus USB1
6PFQ · Uncharacterized protein YLR132C: “Structure of kluyveromyces marxianus USB1”. X-ray diffraction, 6 pockets (best druggability 0.74). MolNFT v1 #160277 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6PFQ
- Type
- protein
- Length
- 640 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein YLR132C
- UniProt
- W0TCJ5
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Uncharacterized protein YLR132C | protein | 212 | 40% helix, 29% strand | W0TCJ5 |
| A | Uncharacterized protein YLR132C | protein | 216 | 39% helix, 28% strand | W0TCJ5 |
| B | Uncharacterized protein YLR132C | protein | 212 | 37% helix, 29% strand | W0TCJ5 |
Ligands and binding sites
- GOL · Glycerol · additive · 11 copies · chains C, A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1150 | 0.74 | 0.77 | 104 | GOL |
| 2 | 291 | 0.59 | 0.78 | 26 | GOL |
| 3 | 282 | 0.57 | 0.77 | 27 | GOL |
| 4 | 165 | 0.52 | 0.79 | 22 | GOL |
| 5 | 108 | 0.45 | 0.79 | 28 | empty |
Interfaces
3 interfaces between chains.
- C–A · 740 Ų buried · 9 hydrogen bonds · protein-protein
- C–B · 323 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 175 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6PFQ · Structure of Kluyveromyces marxianus Usb1 · the same entry in another collection · chain C against C, 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 W0TCJ5
- Elsewhere: RCSB PDB 6PFQ · PDBe 6PFQ · UniProt W0TCJ5
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