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Crystallographic analysis of a complex between human immunodeficiency virus type 1 protease and acetyl-pepstatin at 2.0-ångströms resolution

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PDB: 5HVP
Type: protein
Length: 203 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HIV-1 protease; Acetyl-*pepstatin
UniProt: Q9WFL7
Ligands: ACE, CL

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	HIV-1 protease	protein	99	7% helix, 58% strand	Q9WFL7
C	Acetyl-*pepstatin	protein	5	0% helix, 40% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains A, C
CL · Chloride ion · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

3 interfaces between chains.

A–B · 1857 Å² buried · 37 hydrogen bonds · protein-protein
B–C · 462 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 431 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified, 1 covalent (nonstandard, covalent ligand).

Compared structures

5HVP · Crystallographic analysis of a complex between human immunodeficiency virus type 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 Q9WFL7
Elsewhere: RCSB PDB 5HVP · PDBe 5HVP · UniProt Q9WFL7

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