› 5km5

X-ray diffraction
2.1Å resolution

Human Histidine Triad Nucleotide Binding Protein 2 (hHint2) triciribine 5'-monoposphate catalytic product complex

Released:
DOI: 10.2210/pdb5km5/pdb
PDB 5km5 coloured by chain and viewed from the front.
PDB 5km5 coloured by chain and viewed from the side.
PDB 5km5 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
A Crystal Structure-Based Guide to the Design of Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) Activated ProTides.
Maize KM, Shah R, Strom A, Kumarapperuma S, Zhou A, Wagner CR, Finzel BC
Mol. Pharm. (2017)
PMID: 28968488

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosine 5'-monophosphoramidase HINT2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 142 amino acids
Theoretical weight: 15.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BX68 (Residues: 26-163; Coverage: 85%)
Gene name: HINT2
Sequence domains: HIT domain
Structure domains: HIT-like

Ligands and Environments

3 bound ligands:
Ligand CL 1 x CL
Ligand PG4 1 x PG4
Ligand TR5 1 x TR5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 38.129Å b: 76.045Å c: 77.821Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.171 0.224
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

The Enzyme-Free Release of Nucleotides from Phosphoramidates Depends Strongly on the Amino Acid.
Jovanovic et al. (2020)
1 more

1 mention without citation

Crystal Structure of Histidine Triad Nucleotide-Binding Protein from the Pathogenic Fungus Candida albicans.
Jung et al. (2019)