› 4aif

X-ray diffraction
2.01Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126132 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
AH receptor-interacting protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 144 amino acids
Theoretical weight: 16.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O00170 (Residues: 172-315; Coverage: 44%)
Gene names: AIP, XAP2
Structure domains: Tetratricopeptide repeat domain
Heat shock protein HSP 90-alpha Chains: D, E
Molecule details ›
Chains: D, E
Length: 7 amino acids
Theoretical weight: 866 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P07900 (Residues: 726-732; Coverage: 1%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 63.82Å b: 104.49Å c: 69.27Å
α: 90° β: 97.41° γ: 90°
R-values:
R R work R free
0.19 0.188 0.236
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

10 review citations

Genetic and epigenetic mutations of tumor suppressive genes in sporadic pituitary adenoma.
Zhou et al. (2014)
9 more

9 mentions without citation

Structure of the TPR domain of AIP: lack of client protein interaction with the C-terminal α-7 helix of the TPR domain of AIP is sufficient for pituitary adenoma predisposition.
Morgan et al. (2012)
8 more