Research workbench
X-ray structure of nifs-like protein from rickettsia africae esf-5
Analyse X-ray structure of nifs-like protein from rickettsia africae esf-5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IXO
- Type
- protein
- Length
- 722 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nifs-like protein
- UniProt
- C3PNQ7
- Ligands
- CA
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nifs-like protein | protein | 360 | 41% helix, 16% strand | C3PNQ7 |
| B | Nifs-like protein | protein | 362 | 41% helix, 16% strand | C3PNQ7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.76 | 0.98 | 18 | empty |
| 2 | 62 | 0.72 | 0.98 | 28 | empty |
| 3 | 299 | 0.62 | 0.80 | 38 | empty |
| 4 | 276 | 0.61 | 0.80 | 37 | empty |
| 5 | 68 | 0.38 | 0.79 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2234 Ų buried · 36 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cofactor).
Compared structures
- 4IXO · X-ray structure of NifS-like protein from Rickettsia africae ESF-5 · 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 C3PNQ7
- Elsewhere: RCSB PDB 4IXO · PDBe 4IXO · UniProt C3PNQ7
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