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Crystal structure of an intact type IV self-sufficient cytochrome P450 monooxygenase

Analyse Crystal structure of an intact type IV self-sufficient cytochrome P450… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6KBH
Type: protein
Length: 765 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P450 monooxygenase
UniProt: C7SFP5
Ligands: FMN, HEM, FES
Pockets: 8 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P450 monooxygenase	protein	765	38% helix, 18% strand	C7SFP5

Ligands and binding sites

FMN · Flavin mononucleotide · ligand · chains A
HEM · Protoporphyrin IX containing Fe · ligand · chains A
FES · Fe2/s2 (inorganic) cluster · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	599	0.84	0.89	67	HEM
2	813	0.75	0.79	99	FMN
3	398	0.71	0.82	53	empty
4	329	0.57	0.76	47	empty
5	116	0.51	0.82	26	empty

Compared structures

6KBH · Crystal structure of an intact type IV self-sufficient cytochrome P450 monooxygenase · 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 C7SFP5
Elsewhere: RCSB PDB 6KBH · PDBe 6KBH · UniProt C7SFP5

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