Research workbench
T. atroviride fdc variant tafdcv in complex with hydroxylated prfmn
Analyse T. atroviride fdc variant tafdcv in complex with hydroxylated prfmn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NF0
- Type
- protein
- Length
- 994 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G9NLP8
- Ligands
- BYN, K, MN, NO3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 497 | — | G9NLP8 |
Ligands and binding sites
- BYN · hydroxylated prenyl-FMN · ligand · 2 copies · chains A, B
- K · Potassium ion · metal · 4 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- NO3 · Nitrate ion · ion · chains A
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NF0 · T. atroviride Fdc variant TaFdcV in complex with hydroxylated prFMN · 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 G9NLP8
- Elsewhere: RCSB PDB 7NF0 · PDBe 7NF0 · UniProt G9NLP8
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