MolNFT v1 · #64584 · protein
Crystal structure of a nifx-associated protein of unknown function (AFE_1514) from acidithiobacillus ferrooxidans atcc at 2.00 a resolution
3G7P · Nitrogen fixation protein: “Crystal structure of a nifx-associated protein of unknown function (AFE_1514) from acidithiobacillus…”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.42). MolNFT v1 #64584 on GenesisL1…
- PDB
- 3G7P
- Type
- protein
- Length
- 145 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrogen fixation protein
- UniProt
- B5ER68
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrogen fixation protein | protein | 145 | 55% helix, 16% strand | B5ER68 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- PG6 · 1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.42 | 0.74 | 19 | EDO |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3G7P · Crystal structure of a nifx-associated protein of unknown function (afe_1514) from… · 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 B5ER68
- Elsewhere: RCSB PDB 3G7P · PDBe 3G7P · UniProt B5ER68
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