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1H, 13C, and 15N chemical shift assignments for irtks-SH3 and espfu- R47 complex

Analyse 1H, 13C, and 15N chemical shift assignments for irtks-SH3 and espfu- R47 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2KXC
Type
protein
Length
84 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1; Espf-like…
UniProt
Q9UHR4, Q8X2D5

Structure

solution nmr · 2 distinct chains · 4% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABrain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1protein674% helix, 39% strandQ9UHR4
BEspf-like proteinprotein170% helix, 0% strandQ8X2D5

Interfaces

1 interface between chains.

  • A–B · 603 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 2KXC · 1H, 13C, and 15N Chemical Shift Assignments for IRTKS-SH3 and EspFu-R47 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UHR4 · AlphaFold monomer V2.0 prediction for brain-specific angiogenesis inhibitor 1-associated… · a predicted model of the same protein · chain A against A, TM-score 0.84

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