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HIV-1 protease-inhibitor complex

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

PDB: 2BPZ
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease
EC: 3.4.23.16
UniProt: P04587
Ligands: 3IN
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease (EC 3.4.23.16)	protein	99	7% helix, 58% strand	P04587

Ligands and binding sites

3IN · N-[2(S)-cyclopentyl-1(R)-hydroxy-3(r)methyl]-5-[(2(S)-tertiary-butylamino-carbonyl)-4-(N1-(2)-(N-methylpiperazinyl)-3-chloro-pyrazinyl-5-carbonyl)-piperazino]-4(S)-hydroxy-2(R)-phenylmethyl-pentanamide · 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	373	0.72	0.84	34	3IN

Interfaces

1 interface between chains.

A–B · 1853 Å² buried · 37 hydrogen bonds · protein-protein

Compared structures

2BPZ · HIV-1 protease-inhibitor complex · 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 2BPZ · PDBe 2BPZ · UniProt P04587

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