Research workbench
Ng domain of human SRP54 T117 deletion mutant
Analyse Ng domain of human SRP54 T117 deletion mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y31
- Type
- protein
- Length
- 1,175 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal recognition particle 54 kda protein
- UniProt
- P61011
- Pockets
- 17 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal recognition particle 54 kda protein | protein | 290 | 50% helix, 13% strand | P61011 |
| B, C, D | Signal recognition particle 54 kda protein | protein | 295 | 52% helix, 14% strand | P61011 |
Pockets
17 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.58 | 0.73 | 54 | empty |
| 2 | 462 | 0.57 | 0.73 | 58 | empty |
| 3 | 104 | 0.55 | 0.84 | 22 | empty |
| 4 | 111 | 0.48 | 0.80 | 24 | empty |
| 5 | 116 | 0.48 | 0.80 | 25 | empty |
Interfaces
2 interfaces between chains.
- A–B · 546 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 545 Ų buried · 2 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 P61011
- Elsewhere: RCSB PDB 6Y31 · PDBe 6Y31 · UniProt P61011
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