Research workbench
Selenomethionine BT4246
Analyse Selenomethionine BT4246 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CK1
- Type
- protein
- Length
- 584 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Susd homolog
- UniProt
- Q89ZX5
- Ligands
- CA
- Pockets
- 4 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Susd homolog | protein | 584 | 41% helix, 10% strand | Q89ZX5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.57 | 0.91 | 21 | empty |
| 2 | 143 | 0.50 | 0.79 | 21 | empty |
| 3 | 159 | 0.49 | 0.77 | 27 | empty |
| 4 | 196 | 0.47 | 0.75 | 21 | empty |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 5CK1 · selenomethionine BT4246 · the same entry in another collection · chain A against A, 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 Q89ZX5
- Elsewhere: RCSB PDB 5CK1 · PDBe 5CK1 · UniProt Q89ZX5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.