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Glycosylation associate protein (GAP123) complex from streptococcus agalactiae

Analyse Glycosylation associate protein (GAP123) complex from streptococcus agalactiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6OYC
Type
protein
Length
1,325 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glycosylation associate protein 1; Glycosylation associate protein 2; Glycosylation…
UniProt
Q8DYM4, Q8DYM5, Q8DYM6
Ligands
SO4
Pockets
20 · best druggability 0.87

Structure

x-ray diffraction · 3 distinct chains · 30% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlycosylation associate protein 1protein49834% helix, 24% strandQ8DYM4
BGlycosylation associate protein 2protein51731% helix, 31% strandQ8DYM5
CGlycosylation associate protein 3protein31023% helix, 30% strandQ8DYM6

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, B
  • GOL · Glycerol · additive · 13 copies · chains A, B, C

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

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110510.870.8893empty
24430.670.7950GOL
33850.630.7845GOL
41440.630.8631empty
51950.590.8142empty

Interfaces

3 interfaces between chains.

  • A–C · 2320 Ų buried · 37 hydrogen bonds · protein-protein
  • B–C · 1415 Ų buried · 28 hydrogen bonds · protein-protein
  • A–B · 795 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 6OYC · Glycosylation Associate Protein (Gap123) complex from Streptococcus agalactiae · the same entry in another collection · chain A against A, TM-score 1.00

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