MolNFT v1 · #73523 · protein
Structure and catalysis of acylaminoacyl peptidase
3O4I · Acylamino-acid-releasing enzyme: “Structure and catalysis of acylaminoacyl peptidase”. X-ray diffraction, 1 ligand (CL), 10 pockets (best druggability 0.77). MolNFT v1 #73523 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3O4I
- Type
- protein
- Length
- 1,152 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acylamino-acid-releasing enzyme
- EC
- 3.4.19.1
- UniProt
- Q9YBQ2
- Ligands
- CL
- Pockets
- 10 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acylamino-acid-releasing enzyme (EC 3.4.19.1) | protein | 576 | 22% helix, 40% strand | Q9YBQ2 |
| B | Acylamino-acid-releasing enzyme (EC 3.4.19.1) | protein | 576 | 22% helix, 40% strand | Q9YBQ2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.77 | 0.88 | 42 | GOL |
| 2 | 982 | 0.74 | 0.77 | 109 | GOL |
| 3 | 936 | 0.73 | 0.77 | 99 | empty |
| 4 | 120 | 0.43 | 0.77 | 23 | empty |
| 5 | 116 | 0.43 | 0.77 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1142 Ų buried · 10 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 Q9YBQ2
- Elsewhere: RCSB PDB 3O4I · PDBe 3O4I · UniProt Q9YBQ2
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