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Structure of full-length extracellular domain of hai-1 at pH 4.6

Analyse Structure of full-length extracellular domain of hai-1 at pH 4.6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5H7V
Type
protein
Length
320 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Kunitz-type protease inhibitor 1
UniProt
O43278
Pockets
4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AKunitz-type protease inhibitor 1protein32012% helix, 25% strandO43278

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110850.760.7876empty
21110.720.9220empty
33150.690.8339empty
4680.520.8520empty

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 5H7V · Structure of full-length extracellular domain of HAI-1 at pH 4.6 · the same entry in another collection · chain A against A, TM-score 1.00
  • O43278 · AlphaFold monomer V2.0 prediction for kunitz-type protease inhibitor 1 (O43278) · a predicted model of the same protein · chain A against A, TM-score 0.94

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