MolNFT v1 · #117756 · protein
Indirect contributions of mutations underlie optimization of new enzyme function
5EHT · N-acyl homoserine lactonase: “Indirect contributions of mutations underlie optimization of new enzyme function”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.61). MolNFT v1 #117756 on GenesisL1: 3D structure…
- PDB
- 5EHT
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acyl homoserine lactonase
- EC
- 3.1.1.81
- UniProt
- A3FJ64
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acyl homoserine lactonase (EC 3.1.1.81) | protein | 253 | 25% helix, 30% strand | A3FJ64 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.61 | 0.84 | 26 | GOL |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 5EHT · Indirect contributions of mutations underlie optimization of new enzyme function · the same entry in another collection · chain A against A, TM-score 1.00
- A3FJ64 · AlphaFold monomer V2.0 prediction for N-acyl homoserine lactonase (A3FJ64) · 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 A3FJ64
- Elsewhere: RCSB PDB 5EHT · PDBe 5EHT · UniProt A3FJ64
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