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Crystal structure of HIV protease complexed with arylsulfonamide azacyclic urea

Analyse Crystal structure of HIV protease complexed with arylsulfonamide azacyclic urea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T7K
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein [contains: protease (retropepsin)]
EC: 3.4.23.16
UniProt: P03368
Ligands: BH0
Pockets: 1 · best druggability 0.75

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein [contains: protease (retropepsin)] (EC 3.4.23.16)	protein	99	7% helix, 54% strand	P03368

Ligands and binding sites

BH0 · 3-({5-benzyl-6-hydroxy-2,4-bis-(4-hydroxy-benzyl)-3-oxo-[1,2,4]-triazepane-1-sulfonyl)-benzonitrile · 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	361	0.75	0.86	36	BH0

Interfaces

1 interface between chains.

A–B · 1855 Å² buried · 42 hydrogen bonds · protein-protein

Compared structures

1T7K · Crystal Structure of HIV Protease complexed with Arylsulfonamide azacyclic urea · 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 P03368
Elsewhere: RCSB PDB 1T7K · PDBe 1T7K · UniProt P03368

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