MolNFT v1 · #134866 · protein
Comprehensive analysis of a novel ketoreductase for pentangular polyphenol biosynthesis
5THQ: “Comprehensive analysis of a novel ketoreductase for pentangular polyphenol biosynthesis”. X-ray diffraction, 1 ligand (NDP). MolNFT v1 #134866 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5THQ
- Type
- protein
- Length
- 1,996 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A023PKG5
- Ligands
- NDP
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G, A | — | protein | 248 | — | A0A023PKG5 |
| B, C, F, E, H, D | — | protein | 250 | — | A0A023PKG5 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · 8 copies · chains G, B, C, F, A, E, H, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5THQ · Comprehensive Analysis of a Novel Ketoreductase for Pentangular Polyphenol Biosynthesis · the same entry in another collection · chain G against G, 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 A0A023PKG5
- Elsewhere: RCSB PDB 5THQ · PDBe 5THQ · UniProt A0A023PKG5
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