Research workbench
Crystal structure of human peptidyl-prolyl cis-trans isomerase FKBP14
Analyse Crystal structure of human peptidyl-prolyl cis-trans isomerase FKBP14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DIP
- Type
- protein
- Length
- 1,201 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP14
- EC
- 5.2.1.8
- UniProt
- Q9NWM8
- Ligands
- NA, PO4
- Pockets
- 14 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 12% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peptidyl-prolyl cis-trans isomerase FKBP14 (EC 5.2.1.8) | protein | 121 | 13% helix, 36% strand | Q9NWM8 |
| C, D, E, F, G | Peptidyl-prolyl cis-trans isomerase FKBP14 (EC 5.2.1.8) | protein | 120 | 11% helix, 36% strand | Q9NWM8 |
| H, J | Peptidyl-prolyl cis-trans isomerase FKBP14 (EC 5.2.1.8) | protein | 119 | 11% helix, 36% strand | Q9NWM8 |
| I | Peptidyl-prolyl cis-trans isomerase FKBP14 (EC 5.2.1.8) | protein | 121 | 13% helix, 36% strand | Q9NWM8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.75 | 0.79 | 87 | empty |
| 2 | 927 | 0.69 | 0.74 | 85 | empty |
| 3 | 497 | 0.62 | 0.75 | 32 | empty |
| 4 | 371 | 0.62 | 0.78 | 36 | empty |
| 5 | 261 | 0.55 | 0.76 | 30 | empty |
Interfaces
20 interfaces between chains.
- I–J · 652 Ų buried · 9 hydrogen bonds · protein-protein
- B–F · 547 Ų buried · 5 hydrogen bonds · protein-protein
- A–H · 534 Ų buried · 4 hydrogen bonds · protein-protein
- H–I · 514 Ų buried · 7 hydrogen bonds · protein-protein
- C–E · 504 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 4DIP · Crystal structure of human Peptidyl-prolyl cis-trans isomerase FKBP14 · the same entry in another collection · chain J against J, TM-score 1.00
- Q9NWM8 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP14 (Q9NWM8) · a predicted model of the same protein · chain E against A, TM-score 0.98
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 Q9NWM8
- Elsewhere: RCSB PDB 4DIP · PDBe 4DIP · UniProt Q9NWM8
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