MolNFT v1 · #33063 · protein
Insights into the role of nucleotide-dependent conformational change in nitrogenase catalysis: structural characterization of the nitrogenase fe protein LEU127 deletion variant with bound mgatp
2C8V · Nitrogenase iron protein 1: “Insights into the role of nucleotide-dependent conformational change in nitrogenase catalysis: structural…”. X-ray diffraction, 3 ligands (FES, ATP, MG), 3 pockets (best druggability 0.37). MolNFT v1…
- PDB
- 2C8V
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrogenase iron protein 1
- EC
- 1.18.6.1
- UniProt
- P00459
- Ligands
- FES, ATP, MG
- Pockets
- 3 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrogenase iron protein 1 (EC 1.18.6.1) | protein | 271 | 37% helix, 15% strand | P00459 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 2 copies · chains A
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.37 | 0.76 | 18 | ATP |
| 2 | 94 | 0.35 | 0.75 | 16 | empty |
| 3 | 73 | 0.31 | 0.74 | 21 | MG |
Compared structures
- 2C8V · Insights into the role of nucleotide-dependent conformational change in nitrogenase… · the same entry in another collection · chain A against A, TM-score 1.00
- P00459 · AlphaFold monomer V2.0 prediction for nitrogenase iron protein 1 (P00459) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P00459
- Elsewhere: RCSB PDB 2C8V · PDBe 2C8V · UniProt P00459
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