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Crystal structure of bacillus subtilis protein yhfp
Analyse Crystal structure of bacillus subtilis protein yhfp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TT7
- Type
- protein
- Length
- 1,974 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Yhfp
- UniProt
- O07615
- Pockets
- 12 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Yhfp | protein | 329 | 27% helix, 27% strand | O07615 |
Pockets
12 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1169 | 0.82 | 0.83 | 110 | empty |
| 2 | 1089 | 0.82 | 0.83 | 96 | empty |
| 3 | 1048 | 0.82 | 0.83 | 99 | empty |
| 4 | 729 | 0.80 | 0.84 | 92 | empty |
| 5 | 618 | 0.80 | 0.85 | 75 | empty |
Interfaces
12 interfaces between chains.
- B–E · 1251 Ų buried · 30 hydrogen bonds · protein-protein
- C–F · 1227 Ų buried · 33 hydrogen bonds · protein-protein
- A–D · 1226 Ų buried · 36 hydrogen bonds · protein-protein
- D–F · 512 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 498 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
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 O07615
- Elsewhere: RCSB PDB 1TT7 · PDBe 1TT7 · UniProt O07615
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