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The HIV protease (mutant Q7K L33I L63I) complexed with kni-764 (an inhibitor)

Analyse The HIV protease (mutant Q7K L33I L63I) complexed with kni-764 (an inhibitor) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MSM
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein
EC: 3.4.23.16
UniProt: P03367
Ligands: JE2
Pockets: 1 · best druggability 0.73

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein (EC 3.4.23.16)	protein	99	7% helix, 55% strand	P03367

Ligands and binding sites

JE2 · (4R)-3-{(2S,3S)-2-hydroxy-3-[(3-hydroxy-2-methylbenzoyl)amino]-4-phenylbutanoyl}-5,5-dimethyl-N-(2-methylbenzyl)-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	348	0.73	0.84	43	JE2

Interfaces

1 interface between chains.

A–B · 1872 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

1MSM · The HIV protease (mutant Q7K L33I L63I) complexed with KNI-764 (an inhibitor) · 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 P03367
Elsewhere: RCSB PDB 1MSM · PDBe 1MSM · UniProt P03367

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