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Substrate-free cytochrome P450EPOK

Analyse Substrate-free cytochrome P450EPOK in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q5E
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: P450 epoxidase
UniProt: Q9KIZ4
Ligands: HEM
Pockets: 6 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	P450 epoxidase	protein	404	50% helix, 8% strand	Q9KIZ4

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	837	0.86	0.88	69	HEM
2	104	0.47	0.80	21	empty
3	64	0.38	0.79	19	empty
4	96	0.36	0.74	15	empty
5	74	0.35	0.76	17	empty

Compared structures

1Q5E · Substrate-free Cytochrome P450epoK · the same entry in another collection · chain A against A, TM-score 1.00
Q9KIZ4 · AlphaFold monomer V2.0 prediction for epothilone C/D epoxidase (Q9KIZ4) · a predicted model of the same protein · chain A 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 Q9KIZ4
Elsewhere: RCSB PDB 1Q5E · PDBe 1Q5E · UniProt Q9KIZ4

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