Research workbench
Solution structure of full-length slyd from E.COLI
Analyse Solution structure of full-length slyd from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KFW
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fkbp-type peptidyl-prolyl cis-trans isomerase slyd
- EC
- 5.2.1.8
- UniProt
- P0A9K9
- Pockets
- 1 · best druggability 0.41
Structure
solution nmr · 1 distinct chain · 8% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fkbp-type peptidyl-prolyl cis-trans isomerase slyd (EC 5.2.1.8) | protein | 196 | 8% helix, 25% strand | P0A9K9 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.41 | 0.82 | 11 | empty |
Compared structures
- 2KFW · Solution structure of full-length SlyD from E.coli · the same entry in another collection · chain A against A, TM-score 1.00
- P0A9K9 · AlphaFold monomer V2.0 prediction for fkbp-type peptidyl-prolyl cis- trans isomerase slyd… · a predicted model of the same protein · chain A against A, TM-score 0.50
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 P0A9K9
- Elsewhere: RCSB PDB 2KFW · PDBe 2KFW · UniProt P0A9K9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.