Research workbench
Structural characterization of mutated nrea protein in nitrate binding site from staphylococcus aureus
Analyse Structural characterization of mutated nrea protein in nitrate binding site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IZJ
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nrea
- UniProt
- A0A0D1FZV0
- Ligands
- NO3
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nrea | protein | 138 | 32% helix, 29% strand | A0A0D1FZV0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.56 | 0.81 | 22 | empty |
Compared structures
- 6IZJ · Structural characterization of mutated NreA protein in nitrate binding site 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 A0A0D1FZV0
- Elsewhere: RCSB PDB 6IZJ · PDBe 6IZJ · UniProt A0A0D1FZV0
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