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Structure of HIV-1 protease in complex with potent inhibitor kni-272 determined by neutron crystallography

Analyse Structure of HIV-1 protease in complex with potent inhibitor kni-272 determined… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZYE
Type: protein
Length: 198 residues
Chains: 2
Method: neutron diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
EC: 3.4.23.16
UniProt: Q9EKL4
Ligands: KNI
Pockets: 1 · best druggability 0.74

Structure

neutron 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	Q9EKL4

Ligands and binding sites

KNI · (4R)-N-tert-butyl-3-[(2S,3S)-2-hydroxy-3-({N-[(isoquinolin-5-yloxy)acetyl]-S-methyl-L-cysteinyl}amino)-4-phenylbutanoyl]-1,3-thiazolidine-4-carboxamide · 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	413	0.74	0.84	38	KNI

Interfaces

1 interface between chains.

A–B · 1884 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

2ZYE · Structure of HIV-1 Protease in Complex with Potent Inhibitor KNI-272 Determined by… · 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 Q9EKL4
Elsewhere: RCSB PDB 2ZYE · PDBe 2ZYE · UniProt Q9EKL4

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