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Mouse glandular kallikrein-13 (prorenin converting enzyme)

Analyse Mouse glandular kallikrein-13 (prorenin converting enzyme) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1AO5
Type
protein
Length
472 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glandular kallikrein-13
EC
3.4.21.35
UniProt
P36368
Ligands
NAG
Pockets
1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BGlandular kallikrein-13 (EC 3.4.21.35)protein23611% helix, 33% strandP36368

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B

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
19790.780.8077empty

Interfaces

1 interface between chains.

  • A–B · 820 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 1AO5 · Mouse glandular kallikrein-13 (prorenin converting enzyme) · the same entry in another collection · chain A against A, TM-score 1.00
  • P36368 · AlphaFold monomer V2.0 prediction for epidermal growth factor-binding protein type B… · a predicted model of the same protein · chain A against A, TM-score 1.00

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