Structure of phqe D166N REDUCTASE/DIELS-alderase from penicillium fellutanum in complex with NADP+ and substrate

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

Ligands and binding sites

• NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 6 copies · chains A, B, C, D, E, F
• ZWP · 3-{[2-(2-methylbut-3-en-2-yl)-1H-indol-3-yl]methyl}-8H-pyrrolo[1,2-a]pyrazin-5-ium-1-olate · ligand · chains A

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

Pockets

15 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Interfaces

9 interfaces between chains.

• A–B · 1548 Ų buried · 13 hydrogen bonds · protein-protein
• C–D · 1541 Ų buried · 13 hydrogen bonds · protein-protein
• B–D · 1479 Ų buried · 18 hydrogen bonds · protein-protein
• A–C · 1470 Ų buried · 14 hydrogen bonds · protein-protein
• B–E · 769 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

• 6NKM · Structure of PhqE D166N Reductase/Diels-Alderase from Penicillium fellutanum in complex… · the same entry in another collection · chain C against C, TM-score 1.00
• L0E2Z4 · AlphaFold monomer V2.0 prediction for short-chain DEHYDROGENASE/REDUCTASE phqe (L0E2Z4) · a predicted model of the same protein · 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 L0E2Z4
• Elsewhere: RCSB PDB 6NKM · PDBe 6NKM · UniProt L0E2Z4