Research workbench
E. COLI peptidyl-prolyl cis-trans isomerase, mutant PHE27CF3- TYR/PHE98CF3-tyr
Analyse E. COLI peptidyl-prolyl cis-trans isomerase, mutant PHE27CF3- TYR/PHE98CF3-tyr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N3J
- Type
- protein
- Length
- 337 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase B
- EC
- 5.2.1.8
- UniProt
- P23869
- Pockets
- 3 · best druggability 0.43
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase B (EC 5.2.1.8) | protein | 168 | 15% helix, 33% strand | P23869 |
| B | Peptidyl-prolyl cis-trans isomerase B (EC 5.2.1.8) | protein | 169 | 15% helix, 33% strand | P23869 |
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 | 150 | 0.43 | 0.75 | 25 | empty |
| 2 | 91 | 0.37 | 0.75 | 26 | empty |
| 3 | 55 | 0.27 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 524 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 7N3J · E. coli peptidyl-prolyl cis-trans isomerase, mutant Phe27CF3-Tyr/Phe98CF3-Tyr · the same entry in another collection · chain A against A, TM-score 1.00
- P23869 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase B (P23869) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P23869
- Elsewhere: RCSB PDB 7N3J · PDBe 7N3J · UniProt P23869
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