Research workbench
Biochemical roles for conserved residues in the bacterial fatty acid binding protein family
Analyse Biochemical roles for conserved residues in the bacterial fatty acid binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4X9X
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Degv domain-containing protein MW1315
- UniProt
- Q8NWR0
- Ligands
- OLA
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Degv domain-containing protein MW1315 | protein | 268 | 40% helix, 27% strand | Q8NWR0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.80 | 0.96 | 33 | OLA |
| 2 | 154 | 0.50 | 0.79 | 23 | empty |
| 3 | 96 | 0.45 | 0.79 | 18 | empty |
Compared structures
- 4X9X · Biochemical Roles for Conserved Residues in the Bacterial Fatty Acid Binding Protein… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NWR0 · AlphaFold monomer V2.0 prediction for degv domain-containing protein MW1315 (Q8NWR0) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q8NWR0
- Elsewhere: RCSB PDB 4X9X · PDBe 4X9X · UniProt Q8NWR0
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