Research workbench
Crystal structure analysis of the prolyl aminopeptidase from serratia marcescens
Analyse Crystal structure analysis of the prolyl aminopeptidase from serratia marcescens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QTR
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prolyl aminopeptidase
- EC
- 3.4.11.5
- UniProt
- O32449
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl aminopeptidase (EC 3.4.11.5) | protein | 314 | 43% helix, 16% strand | O32449 |
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 | 376 | 0.68 | 0.81 | 46 | empty |
| 2 | 50 | 0.25 | 0.73 | 12 | empty |
Compared structures
- 1QTR · Crystal structure analysis of the prolyl aminopeptidase from serratia marcescens · 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 0.99
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 1QTR · PDBe 1QTR · UniProt O32449
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