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Structure of HIV pr resistant patient derived mutant (comprising 22 mutations) in complex with drv

Analyse Structure of HIV pr resistant patient derived mutant (comprising 22 mutations)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3T3C
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
P03367
Ligands
017, SO4
Pockets
1 · best druggability 0.68

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHIV-1 protease (EC 3.4.23.16)protein997% helix, 55% strandP03367

Ligands and binding sites

  • 017 · (3r,3as,6ar)-hexahydrofuro[2,3-b]furan-3-yl(1s,2r)-3-[[(4-aminophenyl)sulfonyl](isobutyl)amino]-1-benzyl-2-hydroxypropylcarbamate · ligand · chains A, B
  • SO4 · Sulfate ion · ion · 2 copies · chains A, B
  • BME · Beta-mercaptoethanol · additive · 2 copies · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13850.680.8138017, SO4

Interfaces

1 interface between chains.

  • A–B · 1808 Ų buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (additive adduct).

Compared structures

  • 3T3C · Structure of HIV PR resistant patient derived mutant (comprising 22 mutations) in complex… · the same entry in another collection · chain B against B, TM-score 1.00

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