Research workbench
E. COLI peptidyl-prolyl cis-trans isomerase, mutant PHE4ALA PHE27CF3- PHE/PHE98CF3-phe
Analyse E. COLI peptidyl-prolyl cis-trans isomerase, mutant PHE4ALA PHE27CF3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RFD
- Type
- protein
- Length
- 170 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- J7QN08
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 170 | 14% helix, 35% strand | J7QN08 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.28 | 0.74 | 20 | empty |
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 7RFD · E. coli peptidyl-prolyl cis-trans isomerase, mutant Phe4Ala Phe27CF3-Phe/Phe98CF3-Phe · 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 J7QN08
- Elsewhere: RCSB PDB 7RFD · PDBe 7RFD · UniProt J7QN08
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