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Crystal structure of the N-terminal domain of HIV-1 capsid in complex with inhibitor bi-1

Analyse Crystal structure of the N-terminal domain of HIV-1 capsid in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4J93
Type: protein
Length: 146 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gag protein
UniProt: Q79791
Ligands: 0OE, 1JR
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gag protein	protein	146	58% helix, 4% strand	Q79791

Ligands and binding sites

0OE · 4-{2-[5-(3-chlorophenyl)-1H-pyrazol-4-yl]-1-[3-(1H-imidazol-1-yl)propyl]-1H-benzimidazol-5-yl}benzoic acid · ligand · chains A
1JR · (4S)-3-phenyl-4-(pyridin-3-yl)-4,5-dihydropyrrolo[3,4-c]pyrazol-6(2H)-one · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.32	0.76	12	1JR

Compared structures

4J93 · Crystal Structure of the N-Terminal Domain of HIV-1 Capsid in Complex With Inhibitor BI-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 Q79791
Elsewhere: RCSB PDB 4J93 · PDBe 4J93 · UniProt Q79791

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