Research workbench
Crystal structure of the apo-ysxc
Analyse Crystal structure of the apo-ysxc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SUL
- Type
- protein
- Length
- 381 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding protein ysxc
- UniProt
- P38424
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GTP-binding protein ysxc | protein | 186 | 39% helix, 23% strand | P38424 |
| B | GTP-binding protein ysxc | protein | 195 | 37% helix, 22% strand | P38424 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.52 | 0.80 | 27 | empty |
| 2 | 84 | 0.36 | 0.75 | 11 | empty |
| 3 | 82 | 0.34 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 397 Ų buried · 7 hydrogen bonds · protein-protein
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 P38424
- Elsewhere: RCSB PDB 1SUL · PDBe 1SUL · UniProt P38424
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