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Crystal structure of the laminin-binding protein lbp of streptococcus pyogenes

Analyse Crystal structure of the laminin-binding protein lbp of streptococcus pyogenes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3GI1
Type
protein
Length
508 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Laminin-binding protein of group a streptococci
UniProt
Q7DII5
Ligands
ZN
Pockets
3 · best druggability 0.66

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALaminin-binding protein of group a streptococciprotein25445% helix, 15% strandQ7DII5
BLaminin-binding protein of group a streptococciprotein25446% helix, 15% strandQ7DII5

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15610.660.7769empty
22060.460.7426empty
3760.330.7522empty

Interfaces

1 interface between chains.

  • A–B · 450 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 3GI1 · Crystal Structure of the laminin-binding protein Lbp of Streptococcus pyogenes · the same entry in another collection · chain A against A, TM-score 1.00

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