MolNFT v1 · #100893 · protein
Crystal structure of fosb from staphylococcus aureus at 1.89 ångström resolution - apo structure
4NB2 · Metallothiol transferase fosb: “Crystal structure of fosb from staphylococcus aureus at 1.89 ångström resolution - apo structure”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.52). MolNFT v1 #100893 on…
- PDB
- 4NB2
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallothiol transferase fosb
- EC
- 2.5.1.-
- UniProt
- P60864
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metallothiol transferase fosb (EC 2.5.1.-) | protein | 119 | 24% helix, 39% strand | P60864 |
| B | Metallothiol transferase fosb (EC 2.5.1.-) | protein | 125 | 25% helix, 38% strand | P60864 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 207 | 0.52 | 0.77 | 33 | empty |
| 2 | 120 | 0.49 | 0.80 | 25 | empty |
| 3 | 94 | 0.35 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2641 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 4NB2 · Crystal Structure of FosB from Staphylococcus aureus at 1.89 Angstrom Resolution - Apo… · the same entry in another collection · chain A against A, TM-score 1.00
- P60864 · AlphaFold monomer V2.0 prediction for metallothiol transferase fosb (P60864) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P60864
- Elsewhere: RCSB PDB 4NB2 · PDBe 4NB2 · UniProt P60864
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