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Crystal structure of human lithostathine to 1.3 a resolution

Analyse Crystal structure of human lithostathine to 1.3 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1QDD
Type
protein
Length
144 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lithostathine
UniProt
P05451
Ligands
NDG, GAL, SIA

Structure

x-ray diffraction · 1 distinct chain · 20% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALithostathineprotein14420% helix, 29% strandP05451

Ligands and binding sites

  • NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
  • GAL · beta-D-galactopyranose · sugar · chains A
  • SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A

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

Modifications

Observed in the structure: 3 disulfide, 1 glycan (disulfide, O-glycosylation).

Compared structures

  • 1QDD · Crystal structure of human lithostathine to 1.3 a resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • P05451 · AlphaFold monomer V2.0 prediction for lithostathine-1-alpha (P05451) · a predicted model of the same protein · chain A against A, TM-score 0.91

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