Research workbench
The crystal structure of prolyl aminopeptidase complexed with ala-tboda
Analyse The crystal structure of prolyl aminopeptidase complexed with ala-tboda in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X2E
- Type
- protein
- Length
- 313 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proline iminopeptidase
- EC
- 3.4.11.5
- UniProt
- O32449
- Ligands
- ATX
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline iminopeptidase (EC 3.4.11.5) | protein | 313 | 45% helix, 16% strand | O32449 |
Ligands and binding sites
- ATX · (2S)-2-amino-1-(5-tert-butyl-1,3,4-oxadiazol-2-yl)propan-1-one · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 361 | 0.69 | 0.82 | 47 | ATX |
| 2 | 57 | 0.28 | 0.74 | 12 | empty |
Compared structures
- 1X2E · The crystal structure of prolyl aminopeptidase complexed with Ala-TBODA · the same entry in another collection · chain A against A, TM-score 1.00
- O32449 · AlphaFold monomer V2.0 prediction for proline iminopeptidase (O32449) · 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 O32449
- Elsewhere: RCSB PDB 1X2E · PDBe 1X2E · UniProt O32449
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