UniProt P16855
Nitrogenase vanadium-iron protein alpha chain (P16855)
Nitrogenase vanadium-iron protein alpha chain (UniProt P16855), EC 1.18.6.1: 8 experimental structures on GenesisL1, 9 ligands bound, 34 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P16855
- Protein
- Nitrogenase vanadium-iron protein alpha chain
- EC
- 1.18.6.1
- Experimental structures
- 8
- Predicted models
- 0
- Ligands
- 9
- Pockets
- 34 · 2 records with a druggable one
Structures
8 records of P16855 in the MolNFT archive: 8 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 5N6Y | Azotobacter vinelandii vanadium nitrogenase | x-ray diffraction | A, D | HCA, 8P8, CO3, CLF | — |
| 5N6Y | Azotobacter vinelandii vanadium nitrogenase | x-ray diffraction | A, D | HCA, 8P8, CO3, CLF | — |
| 7ADR | Co bound as bridging ligand at the active site of vanadium nitrogenase vfe protein | x-ray diffraction | A, D | D6N, HCA, BCT, CMO, CLF | — |
| 7ADY | CO-removed state of the active site of vanadium nitrogenase VFe protein | x-ray diffraction | A, D | D6N, HCA, BCT, H2S, CLF, MG | 17 (best 0.86) |
| 7ADY | Co-removed state of the active site of vanadium nitrogenase vfe protein | x-ray diffraction | A, D | D6N, HCA, BCT, H2S, CLF | — |
| 7AIZ | Vanadium nitrogenase VFe protein, high CO state | x-ray diffraction | A, D | D6N, HCA, BCT, CMO, CLF, MG | 17 (best 0.86) |
| 7AIZ | Vanadium nitrogenase vfe protein, high co state | x-ray diffraction | A, D | D6N, HCA, BCT, CMO, CLF | — |
| P16855 | AlphaFold monomer V2.0 prediction for nitrogenase vanadium-iron protein alpha chain (P16855) | — | — | — |
Ligands
- CLF · FE(8)-S(7) cluster · in 7 records
- HCA · 3-hydroxy-3-carboxy-adipic acid · in 7 records
- BCT · Bicarbonate ion · in 5 records
- D6N · FeV · in 5 records
- CMO · Carbon monoxide · in 3 records
- 8P8 · C Fe7 S8 V · in 2 records
- CO3 · Carbonate ion · in 2 records
- H2S · Hydrosulfuric acid · in 2 records
- MG · Magnesium ion · in 2 records
Elsewhere
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