› 6ylu

X-ray diffraction
1.88Å resolution

14-3-3sigma in complex with BLNKpT152 phosphopeptide crystal structure

Released:
DOI: 10.2210/pdb6ylu/pdb
PDB 6ylu coloured by chain and viewed from the front.
PDB 6ylu coloured by chain and viewed from the side.
PDB 6ylu coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
14-3-3sigma in complex with BLNKpT152 phosphopeptide crystal structure
Soini L, Leysen S, Davis J, Ottmann C
J. Struct. Biol. (2020)

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
14-3-3 protein sigma Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 26.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31947 (Residues: 1-231; Coverage: 93%)
Gene names: HME1, SFN
Sequence domains: 14-3-3 protein
B-cell linker protein Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.3 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q8WV28 (Residues: 147-158; Coverage: 3%)
Gene names: BASH, BLNK, SLP65

Ligands and Environments

1 bound ligand:
Ligand MG 3 x MG
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-003
Spacegroup: C2221
Unit cell:
a: 82.25Å b: 112.11Å c: 62.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.211
Expression systems:
  • Escherichia coli
  • Not provided

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