MolNFT v1 · #31306 · protein

Structure of HIV-1 protease bound to atazanavir

2AQU: “Structure of HIV-1 protease bound to atazanavir”. X-ray diffraction, 1 ligand (DR7), 1 pocket (best druggability 0.69). MolNFT v1 #31306 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2AQU
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: DR7
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease (EC 3.4.23.16)	protein	99	7% helix, 55% strand	P03366

Ligands and binding sites

DR7 · (3S,8S,9S,12S)-3,12-bis(1,1-dimethylethyl)-8-hydroxy-4,11-dioxo-9-(phenylmethyl)-6-[[4-(2-pyridinyl)phenyl]methyl]-2,5, 6,10,13-pentaazatetradecanedioic acid dimethyl ester · 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	387	0.69	0.81	34	DR7

Interfaces

1 interface between chains.

A–B · 1839 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

2AQU · Structure of HIV-1 protease bound to atazanavir · 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 2AQU · PDBe 2AQU · UniProt P03366

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