MolNFT v1 · #53064 · protein
Structure and function of the feob G-domain from methanococcus jannaschii
2WJJ · Ferrous iron transport protein B homolog: “Structure and function of the feob G-domain from methanococcus jannaschii”. X-ray diffraction, 1 ligand (GDP), 2 pockets (best druggability 0.33). MolNFT v1 #53064 on GenesisL1: 3D…
- PDB
- 2WJJ
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferrous iron transport protein B homolog
- UniProt
- Q57986
- Ligands
- GDP
- Pockets
- 2 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferrous iron transport protein B homolog | protein | 168 | 42% helix, 27% strand | Q57986 |
| B | Ferrous iron transport protein B homolog | protein | 166 | 37% helix, 27% strand | Q57986 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 89 | 0.33 | 0.74 | 23 | GDP |
| 2 | 59 | 0.29 | 0.74 | 18 | GDP |
Interfaces
1 interface between chains.
- A–B · 625 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 2WJJ · Structure and function of the FeoB G-domain from Methanococcus jannaschii · the same entry in another collection · chain A against A, TM-score 1.00
- Q57986 · AlphaFold monomer V2.0 prediction for FE(2+) transporter feob (Q57986) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q57986
- Elsewhere: RCSB PDB 2WJJ · PDBe 2WJJ · UniProt Q57986
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