MolNFT v2 · #63966 · protein
Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADH
3FPL: “Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii…”. X-ray diffraction at 1.9. MolNFT v2 #63966 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FPL
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Clostridium beijerinckii; Thermoanaerobacter brockii
- UniProt
- P25984, P14941
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 351 | — | P25984, P14941 |
Compared structures
- 3FPL · Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295… · the same entry in another collection · chain A against A, TM-score 1.00
- P25984 · AlphaFold monomer V2.0 prediction for NADP-dependent isopropanol dehydrogenase (P25984) · a predicted model of the same protein · chain A against A, TM-score 1.00
- P14941 · AlphaFold monomer V2.0 prediction for NADP-dependent isopropanol dehydrogenase (P14941) · a predicted model of the same protein · 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 P25984
- Every structure of UniProt P14941
- Elsewhere: RCSB PDB 3FPL · PDBe 3FPL · UniProt P25984 · UniProt P14941
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