Research workbench
N-acyl amino acid racemase from amycolatopsis sp. ts-1-60: G291D-F323Y mutant in complex with N-acetyl naphthylalanine
Analyse N-acyl amino acid racemase from amycolatopsis sp. ts-1-60: G291D-F323Y mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FJO
- Type
- protein
- Length
- 735 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- EC
- 4.2.1.113
- UniProt
- Q44244
- Ligands
- NPQ, MG
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | (EC 4.2.1.113) | protein | 367 | 38% helix, 22% strand | Q44244 |
| B | (EC 4.2.1.113) | protein | 368 | 38% helix, 23% strand | Q44244 |
Ligands and binding sites
- NPQ · N-acetyl naphthylalanine · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1184 | 0.83 | 0.84 | 99 | empty |
| 2 | 140 | 0.71 | 0.91 | 28 | NPQ |
| 3 | 144 | 0.69 | 0.89 | 29 | NPQ |
Interfaces
1 interface between chains.
- A–B · 1292 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 5FJO · N-acyl amino acid racemase from Amycolatopsis sp. Ts-1-60: G291D- F323Y mutant in complex… · 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 Q44244
- Elsewhere: RCSB PDB 5FJO · PDBe 5FJO · UniProt Q44244
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