Research workbench
Crystal structure analysis of the TM107
Analyse Crystal structure analysis of the TM107 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ILV
- Type
- protein
- Length
- 493 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stationary-phase survival protein sure homolog
- UniProt
- P96112
- Pockets
- 6 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stationary-phase survival protein sure homolog | protein | 246 | 29% helix, 32% strand | P96112 |
| B | Stationary-phase survival protein sure homolog | protein | 247 | 29% helix, 30% strand | P96112 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.48 | 0.77 | 31 | empty |
| 2 | 146 | 0.42 | 0.75 | 24 | empty |
| 3 | 133 | 0.41 | 0.75 | 22 | empty |
| 4 | 98 | 0.40 | 0.76 | 17 | empty |
| 5 | 120 | 0.39 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 294 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 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 P96112
- Elsewhere: RCSB PDB 1ILV · PDBe 1ILV · UniProt P96112
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