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Active-site mobility in human immunodeficiency virus type 1 protease as demonstrated by crystal structure of A28S mutant

Analyse Active-site mobility in human immunodeficiency virus type 1 protease as… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AXA
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
EC: 3.4.23.16
UniProt: P03366
Ligands: U0E
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease (EC 3.4.23.16)	protein	99	4% helix, 53% strand	P03366

Ligands and binding sites

U0E · N-[[1-[N-acetamidyl]-[1-cyclohexylmethyl-2-hydroxy-4-isopropyl]-but-4-yl]-carbonyl]-glutaminyl-arginyl-amide · ligand · 2 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	380	0.69	0.82	33	U0E

Interfaces

1 interface between chains.

A–B · 1886 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

1AXA · Active-site mobility in human immunodeficiency virus type 1 protease as demonstrated by… · 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 P03366
Elsewhere: RCSB PDB 1AXA · PDBe 1AXA · UniProt P03366

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