Research workbench
2.75 ångström resolution crystal structure of uncharacterized protein from bacillus cereus atcc 10987
Analyse 2.75 ångström resolution crystal structure of uncharacterized protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F2H
- Type
- protein
- Length
- 612 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q739P5
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 304 | 53% helix, 16% strand | Q739P5 |
| B | Uncharacterized protein | protein | 308 | 53% helix, 16% strand | Q739P5 |
Ligands and binding sites
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.61 | 0.77 | 40 | TRS |
| 2 | 321 | 0.59 | 0.77 | 40 | TRS |
| 3 | 92 | 0.42 | 0.79 | 14 | empty |
| 4 | 59 | 0.28 | 0.74 | 14 | empty |
| 5 | 62 | 0.28 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2818 Ų buried · 36 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 5F2H · 2.75 Angstrom resolution crystal structure of uncharacterized protein from Bacillus… · 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 Q739P5
- Elsewhere: RCSB PDB 5F2H · PDBe 5F2H · UniProt Q739P5
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