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Crystal structure of striga hermonthica HTL1 (SHHTL1)

Analyse Crystal structure of striga hermonthica HTL1 (SHHTL1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5Z7W
Type
protein
Length
540 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hyposensitive to light 1
UniProt
A0A0M4AV81
Ligands
MG, NA
Pockets
3 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHyposensitive to light 1protein26947% helix, 18% strandA0A0M4AV81
BHyposensitive to light 1protein27146% helix, 18% strandA0A0M4AV81

Ligands and binding sites

  • MG · Magnesium ion · metal · 3 copies · chains A, B
  • NA · Sodium ion · metal · 3 copies · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11080.660.8923MG, GOL
2750.640.9020GOL
32250.510.7631empty

Interfaces

1 interface between chains.

  • A–B · 667 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 5Z7W · Crystal structure of Striga hermonthica HTL1 (ShHTL1) · the same entry in another collection · chain A against A, TM-score 1.00

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