Research workbench
Crystal structure of yedk
Analyse Crystal structure of yedk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KBU
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sos response-associated protein
- EC
- 3.4.-.-
- UniProt
- A0A2S5ZH06
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Sos response-associated protein (EC 3.4.-.-) | protein | 214 | 25% helix, 35% strand | A0A2S5ZH06 |
| A | Sos response-associated protein (EC 3.4.-.-) | protein | 213 | 24% helix, 35% strand | A0A2S5ZH06 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.55 | 0.79 | 40 | empty |
Interfaces
1 interface between chains.
- B–A · 434 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6KBU · Crystal structure of yedK · 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 A0A2S5ZH06
- Elsewhere: RCSB PDB 6KBU · PDBe 6KBU · UniProt A0A2S5ZH06
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