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Structure of HIV1 protease and HH1_173_3A complex.

Analyse Structure of HIV1 protease and HH1_173_3A complex. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BBB
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
EC: 3.4.23.16
UniProt: Q5RZ09
Ligands: HH1
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease (EC 3.4.23.16)	protein	99	4% helix, 55% strand	Q5RZ09

Ligands and binding sites

HH1 · (3S)-tetrahydrofuran-3-yl (1R)-3-{(2R)-4-[(1S,3S)-3-(2-amino-2-oxoethyl)-2,3-dihydro-1H-inden-1-yl]-2-benzyl-3-oxo-2,3-dihydro-1H-pyrrol-2-yl}-1-benzyl-2-hydroxypropylcarbamate · ligand · 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	360	0.72	0.84	35	HH1

Interfaces

1 interface between chains.

A–B · 1860 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

2BBB · Structure of HIV1 protease and hh1_173_3a complex. · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q5RZ09
Elsewhere: RCSB PDB 2BBB · PDBe 2BBB · UniProt Q5RZ09

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