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Catalytic domain of the antimicrobial peptidase lysostaphin from staphylococcus simulans crystallized in the absence of phosphate

Analyse Catalytic domain of the antimicrobial peptidase lysostaphin from staphylococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4QPB
Type
protein
Length
267 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lysostaphin
EC
3.4.24.75
UniProt
P10547
Ligands
ZN
Pockets
2 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALysostaphin (EC 3.4.24.75)protein13310% helix, 42% strandP10547
BLysostaphin (EC 3.4.24.75)protein13410% helix, 43% strandP10547

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11680.590.8230EDO
21410.580.8326empty

Interfaces

1 interface between chains.

  • A–B · 105 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4QPB · Catalytic domain of the antimicrobial peptidase lysostaphin from Staphylococcus simulans… · the same entry in another collection · chain A against A, TM-score 1.00
  • P10547 · AlphaFold monomer V2.0 prediction for lysostaphin (P10547) · a predicted model of the same protein · chain A against A, TM-score 0.99

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