MolNFT v1 · #49238 · protein

Crystal structure of protease inhibitor, mit-1-KK80 in complex with wild type HIV-1 protease

2QI0: “Crystal structure of protease inhibitor, mit-1-KK80 in complex with wild type HIV-1 protease”. X-ray diffraction, 2 ligands (MZ3, PO4), 1 pocket (best druggability 0.71). MolNFT v1 #49238 on GenesisL1: 3D structure, binding sites…

PDB: 2QI0
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
UniProt: O38732
Ligands: MZ3, PO4
Pockets: 1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease	protein	99	4% helix, 54% strand	O38732

Ligands and binding sites

MZ3 · N-[(1S,2R)-1-benzyl-2-hydroxy-3-{[(3-methoxyphenyl)sulfonyl](2-thienylmethyl)amino}propyl]-3-fluoro-2-methylbenzamide · ligand · chains A, B
PO4 · Phosphate ion · ion · chains A

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	327	0.71	0.84	33	MZ3

Interfaces

1 interface between chains.

A–B · 1848 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

2QI0 · Crystal structure of protease inhibitor, MIT-1-KK80 in complex with wild type HIV-1… · 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 O38732
Elsewhere: RCSB PDB 2QI0 · PDBe 2QI0 · UniProt O38732

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