› 4apo

X-ray diffraction
1.9Å resolution

Function and Biology Details

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-126134 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
AH receptor-interacting protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O00170 (Residues: 166-330; Coverage: 50%)
Gene names: AIP, XAP2
Structure domains: Tetratricopeptide repeat domain
Mitochondrial import receptor subunit TOM20 homolog Chains: D, E
Molecule details ›
Chains: D, E
Length: 6 amino acids
Theoretical weight: 677 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q15388 (Residues: 140-145; Coverage: 4%)
Gene names: KIAA0016, TOMM20

Ligands and Environments

2 bound ligands:
Ligand 12P 1 x 12P
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 60.2Å b: 106.82Å c: 68.47Å
α: 90° β: 100.85° γ: 90°
R-values:
R R work R free
0.184 0.181 0.234
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

10 review citations

Review: The HSP90 molecular chaperone-an enigmatic ATPase.
Pearl LH. (2016)
9 more

4 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)
3 more