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Crystal structure of wild-type HIV-1 protease in complex with AF69

Analyse Crystal structure of wild-type HIV-1 protease in complex with AF69 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SA5
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
UniProt: O38732
Ligands: A69, PO4
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease	protein	99	4% helix, 54% strand	O38732

Ligands and binding sites

A69 · N-{(2S,3R)-4-[(1,3-benzothiazol-6-ylsulfonyl)(3-phenylpropyl)amino]-3-hydroxy-1-phenylbutan-2-yl}-3-hydroxybenzamide · ligand · chains A, B
PO4 · Phosphate ion · ion · 3 copies · chains B
ACT · Acetate ion · additive · 2 copies · 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	378	0.72	0.83	34	A69

Interfaces

1 interface between chains.

A–B · 1835 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

3SA5 · Crystal structure of wild-type HIV-1 protease in complex with AF69 · 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 O38732
Elsewhere: RCSB PDB 3SA5 · PDBe 3SA5 · UniProt O38732

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