Research workbench
Rt xfel structure of cypa solved using celloluse carrier media
Analyse Rt xfel structure of cypa solved using celloluse carrier media in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6U5E
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidyl-prolyl cis-trans isomerase a
- EC
- 5.2.1.8
- UniProt
- P62937
- Pockets
- 1 · best druggability 0.29
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 a (EC 5.2.1.8) | protein | 163 | 14% helix, 34% strand | P62937 |
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 | 54 | 0.29 | 0.75 | 15 | empty |
Compared structures
- 6U5E · RT XFEL structure of CypA solved using celloluse carrier media · 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 P62937
- Elsewhere: RCSB PDB 6U5E · PDBe 6U5E · UniProt P62937
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