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X-ray structure of bikunin from the human inter-alpha-inhibitor complex

Analyse X-ray structure of bikunin from the human inter-alpha-inhibitor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BIK
Type
protein
Length
110 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bikunin
UniProt
P02760
Ligands
NAG, SO4

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABikuninprotein11019% helix, 27% strandP02760

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A

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

Modifications

Observed in the structure: 6 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

  • 1BIK · X-ray structure of bikunin from the human inter-alpha-inhibitor complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P02760 · AlphaFold monomer V2.0 prediction for protein ambp (P02760) · a predicted model of the same protein · chain A against A, TM-score 0.99

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