Research workbench
Structural analysis of protein folding by the methanococcus jannaschii chaperone FKBP26
Analyse Structural analysis of protein folding by the methanococcus jannaschii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PRD
- Type
- protein
- Length
- 223 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fkbp-type peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- Q58235
- Pockets
- 2 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fkbp-type peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 223 | 23% helix, 34% strand | Q58235 |
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 | 77 | 0.33 | 0.74 | 13 | empty |
| 2 | 51 | 0.30 | 0.76 | 12 | empty |
Compared structures
- 3PRD · Structural analysis of protein folding by the Methanococcus jannaschii chaperone FKBP26 · the same entry in another collection · chain A against A, TM-score 1.00
- Q58235 · AlphaFold monomer V2.0 prediction for long-type peptidyl-prolyl cis- trans isomerase… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q58235
- Elsewhere: RCSB PDB 3PRD · PDBe 3PRD · UniProt Q58235
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