MolNFT v1 · #40340 · protein
Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site
2IOD: “Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of…”. X-ray diffraction. MolNFT v1 #40340 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2IOD
- Type
- protein
- Length
- 1,292 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P93799
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 320 | — | P93799 |
| B | — | protein | 326 | — | P93799 |
| C | — | protein | 325 | — | P93799 |
| D | — | protein | 321 | — | P93799 |
Compared structures
- 2IOD · 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 2IOD · PDBe 2IOD · UniProt P93799
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