MolNFT v1 · #47234 · protein
Crystal structure of the mimivirus cyclophilin
2OSE · Probable peptidyl-prolyl cis-trans isomerase: “Crystal structure of the mimivirus cyclophilin”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.34). MolNFT v1 #47234 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2OSE
- Type
- protein
- Length
- 195 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable peptidyl-prolyl cis-trans isomerase
- EC
- 5.2.1.8
- UniProt
- Q5UP71
- Ligands
- CL
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable peptidyl-prolyl cis-trans isomerase (EC 5.2.1.8) | protein | 195 | 16% helix, 29% strand | Q5UP71 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 0.34 | 0.78 | 17 | empty |
Compared structures
- 2OSE · Crystal Structure of the Mimivirus Cyclophilin · 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 Q5UP71
- Elsewhere: RCSB PDB 2OSE · PDBe 2OSE · UniProt Q5UP71
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