› 6nhk

X-ray diffraction
2.78Å resolution

Mortalin nucleotide binding domain in the ADP-bound state

Released:
DOI: 10.2210/pdb6nhk/pdb
PDB entry 6nhk coloured by chain, front view.
PDB entry 6nhk coloured by chain, side view.
PDB entry 6nhk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin.
Moseng MA, Nix JC, Page RC
J Phys Chem B 123 3383-3396 (2019)
PMID: 30933555

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153699 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stress-70 protein, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 41.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P38646 (Residues: 54-429; Coverage: 55%)
Gene names: GRP75, HSPA9, HSPA9B, mt-HSP70
Sequence domains: Hsp70 protein

Ligands and Environments

4 bound ligands:
Ligand ADP 2 x ADP
Ligand PO4 2 x PO4
Ligand MG 2 x MG
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2
Unit cell:
a: 177.263Å b: 60.102Å c: 91.699Å
α: 90° β: 97.56° γ: 90°
R-values:
R R work R free
0.259 0.256 0.296
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Skeletal Phenotypes Due to Abnormalities in Mitochondrial Protein Homeostasis and Import.
Zhao et al. (2020)
2 other articles

3 mentions without citation

Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin.
Moseng et al. (2019)
2 more