MolNFT v1 · #306771 · protein
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase D (Q4P0V4)
Q4P0V4: “AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase D (Q4P0V4)”. 3 pockets (best druggability 0.64). MolNFT v1 #306771 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q4P0V4
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Peptidyl-prolyl cis-trans isomerase D
- UniProt
- Q4P0V4
- Pockets
- 3 · best druggability 0.64
Structure
1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase D | protein | 398 | 44% helix, 14% strand | Q4P0V4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 320 | 0.64 | 0.80 | 35 | empty |
| 2 | 262 | 0.55 | 0.77 | 38 | empty |
| 3 | 176 | 0.47 | 0.76 | 24 | empty |
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 Q4P0V4
- Elsewhere: UniProt Q4P0V4 · AlphaFold DB Q4P0V4
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