MolNFT v1 · #187034 · protein

S. cerevisiae CYP51 complexed with vt-1129

7RYX · Lanosterol 14-alpha demethylase: “S. cerevisiae CYP51 complexed with vt-1129”. X-ray diffraction, 2 ligands (HEM, 81H), 5 pockets (best druggability 0.87). MolNFT v1 #187034 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 7RYX
Type: protein
Length: 528 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lanosterol 14-alpha demethylase
UniProt: A6ZSR0
Ligands: HEM, 81H
Pockets: 5 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lanosterol 14-alpha demethylase	protein	528	52% helix, 10% strand	A6ZSR0

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · chains A
81H · (2R)-2-(2,4-difluorophenyl)-1,1-difluoro-3-(1H-tetrazol-1-yl)-1-{5-[4-(trifluoromethoxy) phenyl]pyridin-2-yl}propan-2-ol · ligand · chains A

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	899	0.87	0.88	80	HEM, 81H
2	263	0.60	0.79	40	empty
3	201	0.57	0.80	40	empty
4	168	0.51	0.78	25	empty
5	55	0.27	0.73	16	empty

Compared structures

7RYX · S. cerevisiae CYP51 complexed with vt-1129 · 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 7RYX · PDBe 7RYX · UniProt A6ZSR0

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