MolNFT v1 · #99503 · protein
TSE3 structure
4M5E · Uncharacterized protein: “TSE3 structure”. X-ray diffraction, 2 ligands (CA, CD), 2 pockets (best druggability 0.42). MolNFT v1 #99503 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4M5E
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q9HYC5
- Ligands
- CA, CD
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 405 | 63% helix, 1% strand | Q9HYC5 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A
- CD · Cadmium ion · metal · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.42 | 0.77 | 26 | GOL |
| 2 | 82 | 0.34 | 0.75 | 16 | empty |
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 Q9HYC5
- Elsewhere: RCSB PDB 4M5E · PDBe 4M5E · UniProt Q9HYC5
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