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Crystal structure of a fimbrial protein (BACOVA_04982) from bacteroides ovatus atcc 8483 at 1.85 a resolution
Analyse Crystal structure of a fimbrial protein (BACOVA_04982) from bacteroides ovatus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EPS
- Type
- protein
- Length
- 497 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- A7M4E1
- Ligands
- CL, SO4
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein | protein | 497 | 16% helix, 32% strand | A7M4E1 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 22 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.57 | 0.80 | 21 | CL, GOL |
| 2 | 93 | 0.38 | 0.76 | 21 | empty |
| 3 | 62 | 0.37 | 0.79 | 23 | empty |
| 4 | 104 | 0.35 | 0.74 | 24 | GOL |
| 5 | 52 | 0.34 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 4EPS · Crystal structure of a fimbrial protein (BACOVA_04982) from Bacteroides ovatus ATCC 8483… · the same entry in another collection · chain A against A, TM-score 1.00
- A7M4E1 · AlphaFold monomer V2.0 prediction for putative fimbrium tip subunit FIM1C (A7M4E1) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 A7M4E1
- Elsewhere: RCSB PDB 4EPS · PDBe 4EPS · UniProt A7M4E1
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