Research workbench
Pseudomonas aeruginosa FK506-binding protein pafkba
Analyse Pseudomonas aeruginosa FK506-binding protein pafkba in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DEK
- Type
- protein
- Length
- 814 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- Q9HYX8
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 204 | 42% helix, 20% strand | Q9HYX8 |
| G, D | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 202 | 44% helix, 19% strand | Q9HYX8 |
| F | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 206 | 42% helix, 18% strand | Q9HYX8 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 710 | 0.68 | 0.76 | 79 | empty |
| 2 | 630 | 0.67 | 0.76 | 67 | empty |
| 3 | 154 | 0.45 | 0.76 | 25 | empty |
| 4 | 66 | 0.42 | 0.79 | 12 | empty |
| 5 | 109 | 0.40 | 0.76 | 22 | empty |
Interfaces
5 interfaces between chains.
- F–D · 2247 Ų buried · 10 hydrogen bonds · protein-protein
- A–G · 2196 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 272 Ų buried · 2 hydrogen bonds · protein-protein
- A–F · 155 Ų buried · 0 hydrogen bonds · protein-protein
- G–D · 51 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7DEK · Pseudomonas aeruginosa FK506-binding protein PaFkbA · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9HYX8
- Elsewhere: RCSB PDB 7DEK · PDBe 7DEK · UniProt Q9HYX8
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