MolNFT v1 · #169795 · protein
The crystal structure of the S154Y mutant carbonyl reductase from leifsonia xyli explains enhanced activity for 3,5- BIS(TRIFLUOROMETHYL)ACETOPHENONE reduction
6XNB: “The crystal structure of the S154Y mutant carbonyl reductase from leifsonia xyli explains enhanced activity…”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #169795 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XNB
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- T2FLN4
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 251 | — | T2FLN4 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XNB · The Crystal Structure of the S154Y Mutant Carbonyl Reductase from Leifsonia xyli Explains… · 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 T2FLN4
- Elsewhere: RCSB PDB 6XNB · PDBe 6XNB · UniProt T2FLN4
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