MolNFT v1 · #166005 · protein
Spectroscopic and structural characterization of a genetically encoded direct sensor for protein-ligand interactions
6UD1 · Streptavidin: “Spectroscopic and structural characterization of a genetically encoded direct sensor for protein-ligand…”. X-ray diffraction, 1 ligand (CL), 2 pockets (best druggability 0.32). MolNFT v1 #166005 on GenesisL1: 3D…
- PDB
- 6UD1
- Type
- protein
- Length
- 242 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptavidin
- UniProt
- P22629
- Ligands
- CL
- Pockets
- 2 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Streptavidin | protein | 120 | 8% helix, 56% strand | P22629 |
| B | Streptavidin | protein | 122 | 7% helix, 55% strand | P22629 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.32 | 0.76 | 18 | empty |
| 2 | 59 | 0.29 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1623 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 6UD1 · Spectroscopic and structural characterization of a genetically encoded direct sensor for… · the same entry in another collection · chain A against A, 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 P22629
- Elsewhere: RCSB PDB 6UD1 · PDBe 6UD1 · UniProt P22629
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