Research workbench
Low resolution structure of wbdd with C-terminal bundle ordered to residue 505
Analyse Low resolution structure of wbdd with C-terminal bundle ordered to residue 505 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UW0
- Type
- protein
- Length
- 501 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wbdd
- UniProt
- A0A446F868
- Ligands
- SAM
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wbdd | protein | 501 | 41% helix, 14% strand | A0A446F868 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
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 | 575 | 0.73 | 0.80 | 62 | empty |
| 2 | 147 | 0.71 | 0.90 | 25 | empty |
| 3 | 310 | 0.65 | 0.81 | 42 | SAM |
| 4 | 283 | 0.60 | 0.78 | 39 | empty |
| 5 | 94 | 0.45 | 0.80 | 15 | empty |
Compared structures
- 4UW0 · Low resolution structure of WbdD with C-terminal bundle ordered to residue 505 · 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 A0A446F868
- Elsewhere: RCSB PDB 4UW0 · PDBe 4UW0 · UniProt A0A446F868
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.