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Hemoglobin (HB2) from trematode fasciola hepatica

Analyse Hemoglobin (HB2) from trematode fasciola hepatica in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2VYW
Type
protein
Length
148 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hemoglobin
Ligands
HEM, OXY
Pockets
1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHemoglobinprotein14878% helix, 0% strand—

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · chains A
  • OXY · Oxygen molecule · ion · chains A

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
12880.750.8730HEM, OXY

Compared structures

  • 2VYW · Hemoglobin (Hb2) from trematode Fasciola hepatica · the same entry in another collection · chain A against A, TM-score 1.00

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