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Secreted aspartic protease from C. albicans

Analyse Secreted aspartic protease from C. albicans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZAP
Type: protein
Length: 341 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Secreted aspartic proteinase
EC: 3.4.23.24
UniProt: P28871
Ligands: A70, ZN
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Secreted aspartic proteinase (EC 3.4.23.24)	protein	341	11% helix, 47% strand	P28871

Ligands and binding sites

A70 · N-ethyl-N-[(4-methylpiperazin-1-yl)carbonyl]-D-phenylalanyl-N-[(1S,2S,4R)-4-(butylcarbamoyl)-1-(cyclohexylmethyl)-2-hyd roxy-5-methylhexyl]-L-norleucinamide · ligand · chains A
ZN · Zinc ion · metal · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	319	0.58	0.76	38	A70

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1ZAP · Secreted aspartic protease from C. albicans · 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 P28871
Elsewhere: RCSB PDB 1ZAP · PDBe 1ZAP · UniProt P28871

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