Research workbench

HIV-1 protease with cyclic sulfamide inhibitor, AHA047

Analyse HIV-1 protease with cyclic sulfamide inhibitor, AHA047 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1G2K
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protease retropepsin
EC: 3.4.23.16
UniProt: P04587
Ligands: NM1
Pockets: 1 · best druggability 0.71

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Protease retropepsin (EC 3.4.23.16)	protein	99	7% helix, 55% strand	P04587

Ligands and binding sites

NM1 · 3-(7-benzyl-4,5-dihydroxy-1,1-dioxo-3,6-bis-phenoxymethyl-1L6-[1,2,7]thiadiazepan-2-ylmethyl)-N-methyl-benzamide · 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	358	0.71	0.83	37	NM1

Interfaces

1 interface between chains.

A–B · 1872 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

1G2K · HIV-1 protease with cyclic sulfamide inhibitor, AHA047 · 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 P04587
Elsewhere: RCSB PDB 1G2K · PDBe 1G2K · UniProt P04587

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