Research workbench
Crystal structure analysis of FKBP52, crystal form III
Analyse Crystal structure analysis of FKBP52, crystal form III in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LAW
- Type
- protein
- Length
- 469 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase FKBP4
- EC
- 5.2.1.8
- UniProt
- Q02790
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase FKBP4 (EC 5.2.1.8) | protein | 235 | 11% helix, 40% strand | Q02790 |
| B | Peptidyl-prolyl cis-trans isomerase FKBP4 (EC 5.2.1.8) | protein | 234 | 12% helix, 38% strand | Q02790 |
Ligands and binding sites
- DMS · Dimethyl sulfoxide · additive · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.62 | 0.81 | 33 | DMS |
| 2 | 138 | 0.45 | 0.76 | 16 | DMS |
Interfaces
1 interface between chains.
- A–B · 219 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4LAW · Crystal Structure Analysis of FKBP52, Crystal Form III · the same entry in another collection · chain A against A, TM-score 1.00
- Q02790 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP4 (Q02790) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 Q02790
- Elsewhere: RCSB PDB 4LAW · PDBe 4LAW · UniProt Q02790
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