MolNFT v1 · #80121 · protein

The crystal structure of protease SAPP1P from candida parapsilosis in complex with the HIV protease inhibitor ritonavir

3TNE · Secreted aspartic protease: “The crystal structure of protease SAPP1P from candida parapsilosis in complex with the HIV protease inhibitor…”. X-ray diffraction, 1 ligand (RIT), 2 pockets (best druggability 0.70). MolNFT v1 #80121 on…

PDB: 3TNE
Type: protein
Length: 678 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Secreted aspartic protease
EC: 3.4.23.24
UniProt: B8YPM3
Ligands: RIT
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Secreted aspartic protease (EC 3.4.23.24)	protein	339	9% helix, 45% strand	B8YPM3

Ligands and binding sites

RIT · Ritonavir · ligand · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	820	0.70	0.76	78	RIT
2	826	0.70	0.76	66	RIT

Interfaces

1 interface between chains.

A–B · 1355 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

3TNE · The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the… · 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 B8YPM3
Elsewhere: RCSB PDB 3TNE · PDBe 3TNE · UniProt B8YPM3

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