MolNFT v1 · #59435 · protein
Binding of two substrate analogue molecules to dihydroflavonol 4-reductase alters the functional geometry of the catalytic site
3BXX: “Binding of two substrate analogue molecules to dihydroflavonol 4-reductase alters the functional geometry of…”. X-ray diffraction. MolNFT v1 #59435 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3BXX
- Type
- protein
- Length
- 1,944 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P93799
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 324 | — | P93799 |
Compared structures
- 3BXX · Binding of two substrate analogue molecules to dihydroflavonol 4-reductase alters the… · 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 P93799
- Elsewhere: RCSB PDB 3BXX · PDBe 3BXX · UniProt P93799
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