Research workbench
Crystal structure of troa-like periplasmic binding protein fepb from veillonella parvula
Analyse Crystal structure of troa-like periplasmic binding protein fepb from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MO9
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic binding protein
- UniProt
- D1BQR9
- Ligands
- TMO
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic binding protein | protein | 349 | 46% helix, 15% strand | D1BQR9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.55 | 0.75 | 35 | TMO |
| 2 | 69 | 0.29 | 0.73 | 11 | empty |
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 4MO9 · Crystal Structure of TroA-like Periplasmic Binding Protein FepB from Veillonella parvula · 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 D1BQR9
- Elsewhere: RCSB PDB 4MO9 · PDBe 4MO9 · UniProt D1BQR9
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