Structure of the CYP102A1 haem domain with N-carboxybenzyl-L-prolyl-L- phenylalanine in complex with (S)-1-tetralylamine

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 11% strand (DSSP).

Ligands and binding sites

• HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
• ZP6 · (2S)-3-phenyl-2-[[(2S)-1-phenylmethoxycarbonylpyrrolidin-2-yl]carbonylamino]propanoic acid · ligand · 2 copies · chains A, B
• STQ · (1~{S})-1,2,3,4-tetrahydronaphthalen-1-amine · ligand · 2 copies · chains A, B
• GOL · Glycerol · additive · 5 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 858 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

• 7CVR · Structure of the CYP102A1 Haem Domain with N-Carboxybenzyl-L-Prolyl-L-Phenylalanine in… · the same entry in another collection · chain A against A, TM-score 1.00
• P14779 · AlphaFold monomer V2.0 prediction for bifunctional cytochrome P450/NADPH--P450 reductase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P14779
• Elsewhere: RCSB PDB 7CVR · PDBe 7CVR · UniProt P14779