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Structure of P450SKY (CYP163B3), a cytochrome P450 from skyllamycin biosynthesis (heme-coordinated expression tag)

Analyse Structure of P450SKY (CYP163B3), a cytochrome P450 from skyllamycin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L0E
Type: protein
Length: 440 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P450 monooxygenase
EC: 1.14.-.-
UniProt: F2YRY7
Ligands: HEM, SO4
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P450 monooxygenase (EC 1.14.-.-)	protein	440	49% helix, 12% strand	F2YRY7

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	819	0.79	0.82	70	HEM
2	505	0.73	0.82	35	empty
3	51	0.25	0.73	13	empty

Compared structures

4L0E · Structure of P450sky (CYP163B3), a cytochrome P450 from skyllamycin biosynthesis… · 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 F2YRY7
Elsewhere: RCSB PDB 4L0E · PDBe 4L0E · UniProt F2YRY7

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