Research workbench

Streptavidin mutant S112R with a biotC5-1 cofactor - an artificial iron hydroxylase

Analyse Streptavidin mutant S112R with a biotC5-1 cofactor - an artificial iron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6Y33
Type: protein
Length: 123 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.49
Source: Streptomyces avidinii
Molecule: Streptavidin
UniProt: P22629
Ligands: O7Q
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · resolution 1.49 · 1 distinct chain · 8% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
AAA	Streptavidin	protein	123	8% helix, 54% strand	P22629

Ligands and binding sites

O7Q · biotC5-1 cofactor · ligand · chains AAA
GOL · Glycerol · additive · chains AAA

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.48	0.80	21	O7Q

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 6Y33 · PDBe 6Y33 · UniProt P22629

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.