Research workbench
Cryoem structure of mammalian acylaminoacyl-peptidase
Analyse Cryoem structure of mammalian acylaminoacyl-peptidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7PX8
- Type
- protein
- Length
- 2,798 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acylamino-acid-releasing enzyme
- UniProt
- P19205
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 16% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acylamino-acid-releasing enzyme | protein | 700 | 15% helix, 35% strand | P19205 |
| C, D | Acylamino-acid-releasing enzyme | protein | 699 | 17% helix, 35% strand | P19205 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1133 | 0.87 | 0.88 | 98 | empty |
| 2 | 1139 | 0.87 | 0.88 | 112 | empty |
| 3 | 944 | 0.81 | 0.83 | 78 | empty |
| 4 | 1114 | 0.79 | 0.81 | 86 | empty |
| 5 | 1064 | 0.79 | 0.80 | 87 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2331 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 2240 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 2140 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 2112 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 299 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 P19205
- Elsewhere: RCSB PDB 7PX8 · PDBe 7PX8 · UniProt P19205
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