Research workbench

Saccharomyces cerevisiae CYP51 (lanosterol 14-alpha demethylase) G73W mutant

Analyse Saccharomyces cerevisiae CYP51 (lanosterol 14-alpha demethylase) G73W mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5ESI
Type: protein
Length: 530 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lanosterol 14-alpha demethylase
UniProt: A6ZSR0
Ligands: HEM
Pockets: 5 · 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	530	52% helix, 11% strand	A6ZSR0

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

5 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	927	0.86	0.88	79	HEM
2	157	0.66	0.86	20	empty
3	203	0.57	0.80	39	empty
4	129	0.44	0.76	25	empty
5	56	0.35	0.78	11	empty

Compared structures

5ESI · Saccharomyces cerevisiae CYP51 (Lanosterol 14-alpha demethylase) G73W mutant · 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 5ESI · PDBe 5ESI · UniProt A6ZSR0

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