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Epidermicin antimicrobial protein from staphylococcus epidermidis

Analyse Epidermicin antimicrobial protein from staphylococcus epidermidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SIF
Type
protein
Length
401 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Epidermicin locus structural protein
UniProt
H9BG66
Ligands
SO4
Pockets
5 · best druggability 0.69

Structure

x-ray diffraction · 4 distinct chains · 82% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, FEpidermicin locus structural proteinprotein5182% helix, 2% strandH9BG66
DEpidermicin locus structural proteinprotein5082% helix, 0% strandH9BG66
E, HEpidermicin locus structural proteinprotein5082% helix, 2% strandH9BG66
GEpidermicin locus structural proteinprotein4781% helix, 0% strandH9BG66

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 8 copies · chains B, G, D, E, F, H

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14920.690.7954empty
24020.670.7941empty
31990.440.7324empty
4840.360.7510empty
5580.330.7613empty

Interfaces

14 interfaces between chains.

  • B–C · 388 Ų buried · 0 hydrogen bonds · protein-protein
  • D–F · 377 Ų buried · 0 hydrogen bonds · protein-protein
  • A–G · 332 Ų buried · 1 hydrogen bond · protein-protein
  • E–H · 256 Ų buried · 1 hydrogen bond · protein-protein
  • A–E · 188 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 6SIF · Epidermicin antimicrobial protein from Staphylococcus epidermidis · the same entry in another collection · chain E against E, TM-score 1.00

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