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Trimeric HIV-1 matrix protein

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

PDB
1HIW
Type
protein
Length
658 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
HIV-1 matrix protein
UniProt
P12493
Ligands
SO4
Pockets
5 · best druggability 0.73

Structure

x-ray diffraction · 6 distinct chains · 66% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHIV-1 matrix proteinprotein11568% helix, 4% strandP12493
BHIV-1 matrix proteinprotein11067% helix, 5% strandP12493
CHIV-1 matrix proteinprotein11368% helix, 4% strandP12493
QHIV-1 matrix proteinprotein10564% helix, 5% strandP12493
RHIV-1 matrix proteinprotein11265% helix, 4% strandP12493
SHIV-1 matrix proteinprotein10361% helix, 5% strandP12493

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 8 copies · chains A, R, B, C, Q, S

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15600.730.8128empty
26490.720.7935empty
3540.330.7715empty
4510.280.7411empty
5520.270.7411empty

Interfaces

7 interfaces between chains.

  • A–R · 703 Ų buried · 10 hydrogen bonds · protein-protein
  • Q–R · 368 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 338 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 322 Ų buried · 6 hydrogen bonds · protein-protein
  • Q–S · 311 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 1HIW · Trimeric HIV-1 matrix protein · the same entry in another collection · chain A against A, TM-score 1.00

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