MolNFT v1 · #49131 · protein
Crystal structure of cryptosporidium parvum cyclophilin type peptidyl- prolyl cis-trans isomerase CGD2_1660 in the presence of dipeptide ala-pro
2QER · Cyclophilin-like protein, putative: “Crystal structure of cryptosporidium parvum cyclophilin type peptidyl- prolyl cis-trans isomerase CGD2_1660…”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.36). MolNFT v1…
- PDB
- 2QER
- Type
- protein
- Length
- 160 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclophilin-like protein, putative
- UniProt
- A3FQ68
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclophilin-like protein, putative | protein | 160 | 14% helix, 34% strand | A3FQ68 |
Ligands and binding sites
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 | 71 | 0.36 | 0.78 | 15 | empty |
Compared structures
- 2QER · Crystal structure of Cryptosporidium parvum cyclophilin type peptidyl-prolyl cis-trans… · 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 A3FQ68
- Elsewhere: RCSB PDB 2QER · PDBe 2QER · UniProt A3FQ68
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