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Structure of prenylagaramide maturation protease paga

Analyse Structure of prenylagaramide maturation protease paga in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4H6W
Type
protein
Length
552 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-terminal cyanobactin protease
UniProt
F5B6Y7
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AN-terminal cyanobactin proteaseprotein27734% helix, 19% strandF5B6Y7
BN-terminal cyanobactin proteaseprotein27534% helix, 21% strandF5B6Y7

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18870.780.8191empty
21450.430.7530empty
31350.430.7525empty

Interfaces

1 interface between chains.

  • A–B · 666 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 4H6W · Structure of Prenylagaramide maturation protease PagA · the same entry in another collection · chain A against A, TM-score 1.00

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