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The role of ILE87 of CYP158A2 in oxidative coupling reaction

Analyse The role of ILE87 of CYP158A2 in oxidative coupling reaction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DE9
Type: protein
Length: 804 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Biflaviolin synthase CYP158A2
EC: 1.14.21.7
UniProt: Q9FCA6
Ligands: HEM, SPM
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Biflaviolin synthase CYP158A2 (EC 1.14.21.7)	protein	402	49% helix, 10% strand	Q9FCA6

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
SPM · Spermine · ligand · chains B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1139	0.81	0.82	94	HEM
2	1146	0.80	0.81	95	HEM
3	1017	0.77	0.79	96	empty
4	126	0.39	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 405 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

Q9FCA6 · AlphaFold monomer V2.0 prediction for biflaviolin synthase CYP158A2 (Q9FCA6) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q9FCA6
Elsewhere: RCSB PDB 5DE9 · PDBe 5DE9 · UniProt Q9FCA6

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