MolNFT v1 · #129516 · protein
Human FKBP5 protein
5OMP · Peptidyl-prolyl cis-trans isomerase FKBP5: “Human FKBP5 protein”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.50). MolNFT v1 #129516 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OMP
- Type
- protein
- Length
- 412 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP5
- EC
- 5.2.1.8
- UniProt
- Q13451
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase FKBP5 (EC 5.2.1.8) | protein | 412 | 42% helix, 24% strand | Q13451 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.50 | 0.74 | 37 | empty |
| 2 | 101 | 0.40 | 0.76 | 18 | empty |
| 3 | 58 | 0.36 | 0.78 | 13 | empty |
Compared structures
- Q13451 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP5 (Q13451) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q13451
- Elsewhere: RCSB PDB 5OMP · PDBe 5OMP · UniProt Q13451
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