MolNFT v1 · #149156 · protein
Photo-driven hydrogen evolution by an artificial hydrogenase utilizing the biotin-streptavidin technology
6FRY: “Photo-driven hydrogen evolution by an artificial hydrogenase utilizing the biotin-streptavidin technology”. X-ray diffraction, 1 ligand (9CO), 1 pocket (best druggability 0.46). MolNFT v1 #149156 on GenesisL1: 3D structure, binding…
- PDB
- 6FRY
- Type
- protein
- Length
- 125 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptavidin
- UniProt
- P22629
- Ligands
- 9CO
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Streptavidin | protein | 125 | 6% helix, 54% strand | P22629 |
Ligands and binding sites
- 9CO · [CoBr(appy)-Biot]Br · ligand · chains 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 89 | 0.46 | 0.80 | 17 | empty |
Compared structures
- 6FRY · Photo-Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the… · 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 6FRY · PDBe 6FRY · UniProt P22629
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