Artificial transfer hydrogenase with a Mn-12 cofactor and Streptavidin S112Y-K121M mutant

Structure

x-ray diffraction · resolution 1.88 · 3 distinct chains · 7% helix, 54% strand (DSSP).

Ligands and binding sites

• WZQ · 5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]-~{N}-[2-(3,4-dihydro-2~{H}-pyrano[2,3-c]pyridin-6-ylmethylamino)ethyl]pentanamide · ligand · 4 copies · chains A, D, B, C
• MN · Manganese (II) ion · metal · 4 copies · chains A, C
• BR · Bromide ion · ion · 4 copies · chains C
• CL · Chloride ion · ion · chains D

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

Pockets

6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• A–B · 1649 Ų buried · 30 hydrogen bonds · protein-protein
• C–D · 1644 Ų buried · 27 hydrogen bonds · protein-protein
• A–D · 528 Ų buried · 4 hydrogen bonds · protein-protein
• B–C · 527 Ų buried · 3 hydrogen bonds · protein-protein
• A–C · 206 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 8P5Y · PDBe 8P5Y · UniProt P22629