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Wild type HIV protease bound with GW0385

Analyse Wild type HIV protease bound with GW0385 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2FDE
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gag-pol polyprotein
EC: 3.4.23.16
UniProt: P03368
Ligands: 385, K
Pockets: 1 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Gag-pol polyprotein (EC 3.4.23.16)	protein	99	7% helix, 51% strand	P03368

Ligands and binding sites

385 · (3r,3as,6ar)-hexahydrofuro[2,3-b]furan-3-yl [(1S,2R)-3-[(1,3-benzodioxol-5-ylsulfonyl)(isobutyl)amino]-2-hydroxy-1-{4-[(2-methyl-1,3-thiazol-4-yl)methoxy]benzyl}propyl]carbamate · ligand · chains A, B
K · Potassium ion · metal · 4 copies · chains A, B

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	396	0.70	0.82	38	385

Interfaces

1 interface between chains.

A–B · 1842 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

2FDE · Wild type HIV protease bound with GW0385 · 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 P03368
Elsewhere: RCSB PDB 2FDE · PDBe 2FDE · UniProt P03368

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