Research workbench
Stid O-mt residues 976-1266
Analyse Stid O-mt residues 976-1266 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ECV
- Type
- protein
- Length
- 564 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stid protein
- UniProt
- Q8RJY3
- Ligands
- SAH, CL
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Stid protein | protein | 278 | 46% helix, 21% strand | Q8RJY3 |
| A | Stid protein | protein | 286 | 46% helix, 21% strand | Q8RJY3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 718 | 0.71 | 0.77 | 56 | SAH, CL |
| 2 | 508 | 0.65 | 0.77 | 45 | SAH |
| 3 | 137 | 0.48 | 0.78 | 21 | empty |
| 4 | 153 | 0.44 | 0.75 | 26 | empty |
| 5 | 85 | 0.35 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- B–A · 1147 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 6ECV · StiD O-MT residues 976-1266 · the same entry in another collection · chain B against B, 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 Q8RJY3
- Elsewhere: RCSB PDB 6ECV · PDBe 6ECV · UniProt Q8RJY3
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