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Structural and energetic determinants for hyperstable variants of GB1 obtained from in-vitro evolution

Analyse Structural and energetic determinants for hyperstable variants of GB1 obtained… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FIL
Type
protein
Length
112 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Immunoglobulin G-binding protein G
UniProt
P19909
Ligands
CA

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BImmunoglobulin G-binding protein Gprotein5630% helix, 43% strandP19909

Ligands and binding sites

  • CA · Calcium ion · metal · chains A, B

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

Interfaces

1 interface between chains.

  • A–B · 504 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (formylation).

Compared structures

  • 3FIL · Structural and energetic determinants for hyperstable variants of GB1 obtained from… · the same entry in another collection · chain A against A, TM-score 1.00
  • P19909 · AlphaFold monomer V2.0 prediction for immunoglobulin G-binding protein G (P19909) · a predicted model of the same protein · chain A against A, TM-score 0.95

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