Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-dependent FMN reductase PA1204 (Q9I4D4)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-dependent FMN reductase PA1204… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9I4D4
- Type
- protein
- Length
- 185 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8c1c449ec7B9135D02DaB674994E53C7934610b5
- UniProt
- Q9I4D4
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 185 | — | Q9I4D4 |
Compared structures
- 1RTT · Crystal structure determination of a putative NADH-dependent reductase using sulfur… · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 1RTT · Crystal structure determination of a putative NADH-dependent reductase using sulfur… · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 1X77 · Crystal structure of a NAD(P)H-dependent FMN reductase complexed with FMN · an experimental structure of the same protein · chain A against B, TM-score 0.93
- 1X77 · Crystal structure of a NAD(P)H-dependent FMN reductase complexed with FMN · an experimental structure of the same protein · chain A against B, TM-score 0.93
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 Q9I4D4
- Elsewhere: UniProt Q9I4D4 · AlphaFold DB Q9I4D4
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