MolNFT v1 · #168733 · protein

Structure of cytochrome P450TCU

6WPL · Cytochrome P-450CAM, subunit of camphor 5-monooxygenase…: “Structure of cytochrome P450TCU”. X-ray diffraction, 3 ligands (HEM, CAH, K), 3 pockets (best druggability 0.86). MolNFT v1 #168733 on GenesisL1: 3D structure, binding sites…

PDB: 6WPL
Type: protein
Length: 406 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cytochrome P-450CAM, subunit of camphor 5-monooxygenase system
UniProt: A0A1B3EAY9
Ligands: HEM, CAH, K
Pockets: 3 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cytochrome P-450CAM, subunit of camphor 5-monooxygenase system	protein	406	50% helix, 11% strand	A0A1B3EAY9

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
CAH · 5-exo-hydroxycamphor · ligand · chains A
K · Potassium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	454	0.86	0.93	49	HEM, CAH
2	75	0.41	0.79	19	empty
3	82	0.39	0.78	16	empty

Compared structures

6WPL · Structure of Cytochrome P450tcu · 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 A0A1B3EAY9
Elsewhere: RCSB PDB 6WPL · PDBe 6WPL · UniProt A0A1B3EAY9

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