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The crystal structure of HTLV protease complexed with the inhibitor kni-10681

Analyse The crystal structure of HTLV protease complexed with the inhibitor kni-10681 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LIT
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease
UniProt: Q82134
Ligands: E15
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease	protein	116	8% helix, 41% strand	Q82134

Ligands and binding sites

E15 · (4R)-3-[(2S,3S)-3-[[(2S)-2-[[(2S)-2-azanyl-2-phenyl-ethanoyl]amino]-3,3-dimethyl-butanoyl]amino]-2-hydroxy-4-phenyl-but anoyl]-5,5-dimethyl-N-[(2R)-3-methylbutan-2-yl]-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	507	0.69	0.79	42	E15

Interfaces

1 interface between chains.

A–B · 2011 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

3LIT · The crystal structure of htlv protease complexed with the inhibitor KNI-10681 · 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 Q82134
Elsewhere: RCSB PDB 3LIT · PDBe 3LIT · UniProt Q82134

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