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Crystal structure of kibra and angiomotin complex

Analyse Crystal structure of kibra and angiomotin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6JJX
Type
protein
Length
276 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein kibra; Peptide from angiomotin
UniProt
Q5SXA9, Q4VCS5
Pockets
2 · best druggability 0.43

Structure

x-ray diffraction · 4 distinct chains · 31% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein kibraprotein11831% helix, 24% strandQ5SXA9
BProtein kibraprotein12739% helix, 22% strandQ5SXA9
DPeptide from angiomotinprotein160% helix, 0% strandQ4VCS5
CPeptide from angiomotinprotein150% helix, 0% strandQ4VCS5

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11730.430.7327empty
2690.270.7214empty

Interfaces

3 interfaces between chains.

  • A–B · 1356 Ų buried · 13 hydrogen bonds · protein-protein
  • B–D · 536 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 401 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 6JJX · Crystal Structure of KIBRA and Angiomotin complex · the same entry in another collection · chain C against C, TM-score 1.00
  • Q5SXA9 · AlphaFold monomer V2.0 prediction for protein kibra (Q5SXA9) · a predicted model of the same protein · chain A against A, TM-score 0.91
  • Q4VCS5 · AlphaFold monomer V2.0 prediction for angiomotin (Q4VCS5) · a predicted model of the same protein · chain C against A, TM-score 0.33

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