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Structure of HBPA2 from haemophilus parasuis

Analyse Structure of HBPA2 from haemophilus parasuis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TPA
Type
protein
Length
507 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heme-binding protein a
UniProt
B0QSS4
Pockets
4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeme-binding protein aprotein50732% helix, 22% strandB0QSS4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17660.740.7967empty
22470.730.8739empty
31800.550.8025empty
41590.470.7620empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3TPA · Structure of HbpA2 from Haemophilus parasuis · the same entry in another collection · chain A against A, TM-score 1.00

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