MolNFT v1 · #187021 · protein

S. cerevisiae CYP51 I471T mutant complexed with voriconazole

7RY9 · Lanosterol 14-alpha demethylase: “S. cerevisiae CYP51 I471T mutant complexed with voriconazole”. X-ray diffraction, 2 ligands (HEM, VOR), 4 pockets (best druggability 0.86). MolNFT v1 #187021 on GenesisL1: 3D structure, binding…

PDB: 7RY9
Type: protein
Length: 527 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lanosterol 14-alpha demethylase
UniProt: A6ZSR0
Ligands: HEM, VOR
Pockets: 4 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lanosterol 14-alpha demethylase	protein	527	52% helix, 11% strand	A6ZSR0

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
VOR · Voriconazole · ligand · chains A
PG4 · Tetraethylene glycol · additive · chains A

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	894	0.86	0.88	87	HEM, VOR
2	203	0.63	0.83	23	empty
3	286	0.59	0.78	50	empty
4	123	0.43	0.76	24	empty

Compared structures

7RY9 · S. CEREVISIAE CYP51 I471T mutant COMPLEXED WITH Voriconazole · 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 A6ZSR0
Elsewhere: RCSB PDB 7RY9 · PDBe 7RY9 · UniProt A6ZSR0

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