MolNFT v1 · #10704 · protein

Inhibitor of HIV protease with unusual binding mode potently inhibiting multi-resistant protease mutants

1IZH · Proteinase: “Inhibitor of HIV protease with unusual binding mode potently inhibiting multi-resistant protease mutants”. X-ray diffraction, 1 ligand (Q50), 1 pocket (best druggability 0.71). MolNFT v1 #10704 on GenesisL1: 3D…

PDB: 1IZH
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Proteinase
EC: 3.4.23.16
UniProt: Q90EB9
Ligands: Q50
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Proteinase (EC 3.4.23.16)	protein	99	7% helix, 54% strand	Q90EB9

Ligands and binding sites

Q50 · {(1S)-1-benzyl-4-[3-carbamoyl-1-(1-carbamoyl-2-phenyl-ethylcarbamoyl)-(S)-propylcarbamoyl]-2-oxo-5-phenyl-pentyl}-carbamic acid tert-butyl 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	313	0.71	0.84	34	Q50

Interfaces

1 interface between chains.

A–B · 1861 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

1IZH · Inhibitor of HIV protease with unusual binding mode potently inhibiting multi-resistant… · 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 Q90EB9
Elsewhere: RCSB PDB 1IZH · PDBe 1IZH · UniProt Q90EB9

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