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Detergent-bound CYP51 from Acanthamoeba castellanii

Analyse Detergent-bound CYP51 from Acanthamoeba castellanii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7UWP
Type: protein
Length: 888 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.95
Source: Acanthamoeba castellanii
Molecule: sterol 14a-demethylase
EC: 1.14.13.70
UniProt: L8GJB3
Ligands: HEM
Pockets: 9 · best druggability 0.86

Structure

x-ray diffraction · resolution 1.95 · 1 distinct chain · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	sterol 14a-demethylase (EC 1.14.13.70)	protein	444	55% helix, 12% strand	L8GJB3

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
LMT · Dodecyl-beta-D-maltoside · additive · 2 copies · chains A, B

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

Pockets

9 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	704	0.86	0.89	82	HEM, LMT
2	639	0.86	0.90	81	HEM, LMT
3	415	0.83	0.90	55	empty
4	232	0.51	0.75	31	empty
5	214	0.50	0.76	31	empty

Interfaces

1 interface between chains.

A–B · 1883 Å² buried · 11 hydrogen bonds · protein-protein

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 L8GJB3
Elsewhere: RCSB PDB 7UWP · PDBe 7UWP · UniProt L8GJB3

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