MolNFT v1 · #20599 · protein
The crystal structure of the D-aminoacylase mutant D366A
1RJQ: “The crystal structure of the D-aminoacylase mutant D366A”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.72). MolNFT v1 #20599 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RJQ
- Type
- protein
- Length
- 474 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-aminoacylase
- EC
- 3.5.1.81
- UniProt
- Q9AGH8
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-aminoacylase (EC 3.5.1.81) | protein | 474 | 31% helix, 22% strand | Q9AGH8 |
Ligands and binding sites
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 | 60 | 0.72 | 0.97 | 23 | ACT |
| 2 | 99 | 0.35 | 0.74 | 15 | empty |
Compared structures
- 1RJQ · The crystal structure of the D-aminoacylase mutant D366A · 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 Q9AGH8
- Elsewhere: RCSB PDB 1RJQ · PDBe 1RJQ · UniProt Q9AGH8
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