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Molecular recognition of cyclic urea HIV protease inhibitors

Analyse Molecular recognition of cyclic urea HIV protease inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HWR
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: P04585
Ligands: 216
Pockets: 1 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease (EC 3.4.23.16)	protein	99	4% helix, 56% strand	P04585

Ligands and binding sites

216 · [4-R-(4-alpha,6-beta,7-beta]-hexahydro-5,6-di(hydroxy)-1,3-di(allyl)-4,7-bisphenylmethyl)-2H-1,3-diazepinone · 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	313	0.67	0.82	32	216

Interfaces

1 interface between chains.

A–B · 1852 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

1HWR · Molecular recognition of cyclic urea HIV protease inhibitors · the same entry in another collection · chain B against B, 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 P04585
Elsewhere: RCSB PDB 1HWR · PDBe 1HWR · UniProt P04585

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