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Crystal structure of the staphylococcus aureus sasg G52-E2-G53 module

Analyse Crystal structure of the staphylococcus aureus sasg G52-E2-G53 module in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4WVE
Type
protein
Length
420 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Surface protein G
UniProt
Q2G2B2
Ligands
CL

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASurface protein Gprotein2140% helix, 55% strandQ2G2B2
BSurface protein Gprotein2060% helix, 57% strandQ2G2B2

Ligands and binding sites

  • CL · Chloride ion · ion · chains A

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

Interfaces

1 interface between chains.

  • A–B · 227 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4WVE · Crystal structure of the Staphylococcus aureus SasG G52-E2-G53 module · the same entry in another collection · chain A against A, TM-score 1.00
  • Q2G2B2 · AlphaFold monomer V2.0 prediction for surface protein G (Q2G2B2) · a predicted model of the same protein · chain B against A, TM-score 0.79

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