streptavidin mutant S112I with an iridium catalyst for CH activation

Structure

x-ray diffraction · resolution 1.85 · 2 distinct chains · 8% helix, 55% strand (DSSP).

Ligands and binding sites

• NOF · tert-butyl 7'-[5-[(3aS,4S,6aR)-2-oxidanylidene-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoylamino]-1-chloranyl-2,3,4,5,6-pentamethyl-spiro[1$l^{8}-iridapentacyclo[2.2.0.0^{1,3}.0^{1,5}.0^{2,6}]hexane-1,2'-3-aza-1-azonia-2$l^{8}-iridatricyclo[6.3.1.0^{4,12}]dodeca-1(11),4,6,8(12),9-pentaene]-3'-carboxylate · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• A–D · 1633 Ų buried · 27 hydrogen bonds · protein-protein
• B–C · 1621 Ų buried · 25 hydrogen bonds · protein-protein
• C–D · 542 Ų buried · 2 hydrogen bonds · protein-protein
• A–B · 534 Ų buried · 3 hydrogen bonds · protein-protein
• B–D · 218 Ų buried · 2 hydrogen bonds · protein-protein

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 8AQX · PDBe 8AQX · UniProt P22629