Co crystal structure of ecr with butryl-CoA

Structure

x-ray diffraction · 4 distinct chains · 37% helix, 22% strand (DSSP).

Ligands and binding sites

• VES · Pyrrolidine · ligand · 5 copies · chains A, B, C, D
• NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 3 copies · chains A, C, B, D
• 2EC · 9-ethyl-9H-purin-6-ylamine · ligand · 2 copies · chains A, B
• YAS · ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{S},3~{R},4~{S},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] butanethioate · ligand · 2 copies · chains A, C, B, D
• NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · ligand · chains C

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

Pockets

19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Interfaces

6 interfaces between chains.

• B–D · 1700 Ų buried · 29 hydrogen bonds · protein-protein
• A–C · 1699 Ų buried · 29 hydrogen bonds · protein-protein
• B–C · 1230 Ų buried · 20 hydrogen bonds · protein-protein
• A–D · 1213 Ų buried · 20 hydrogen bonds · protein-protein
• C–D · 1032 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

• 6NA4 · Co crystal structure of ECR with Butryl-CoA · 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 E4N096
• Elsewhere: RCSB PDB 6NA4 · PDBe 6NA4 · UniProt E4N096