Research workbench
Crystal structure of cyclophilin abh-like domain of human peptidylprolyl isomerase E isoform 1
Analyse Crystal structure of cyclophilin abh-like domain of human peptidylprolyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R99
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase E
- EC
- 5.2.1.8
- UniProt
- Q9UNP9
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase E (EC 5.2.1.8) | protein | 164 | 14% helix, 34% strand | Q9UNP9 |
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 | 51 | 0.30 | 0.77 | 19 | empty |
Compared structures
- 2R99 · Crystal structure of cyclophilin ABH-like domain of human peptidylprolyl isomerase E… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UNP9 · AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase E (Q9UNP9) · a predicted model of the same protein · 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 Q9UNP9
- Elsewhere: RCSB PDB 2R99 · PDBe 2R99 · UniProt Q9UNP9
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