› 5kly

X-ray diffraction
1.3Å resolution

Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) H112N mutant adenosine nucleoside phosphoramidate substrate complex

Released:
DOI: 10.2210/pdb5kly/pdb
PDB entry 5kly coloured by chain, front view.
PDB entry 5kly coloured by chain, side view.
PDB entry 5kly coloured by chain, top view.
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 14 3987-3997 (2017)
PMID: 28968488

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156024 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosine 5'-monophosphoramidase HINT1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 129 amino acids
Theoretical weight: 14.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49773 (Residues: 1-126; Coverage: 100%)
Gene names: HINT, HINT1, PKCI1, PRKCNH1
Sequence domains: HIT domain
Structure domains: HIT-like

Ligands and Environments

3 bound ligands:
Ligand 6UR 1 x 6UR
Ligand PEG 1 x PEG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: C2
Unit cell:
a: 77.865Å b: 46.502Å c: 64.063Å
α: 90° β: 94.8° γ: 90°
R-values:
R R work R free
0.15 0.148 0.171
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Prodrugs of Nucleoside 5'-Monophosphate Analogues: Overview of the Recent Literature Concerning their Synthesis and Applications.
Roy et al. (2023)
1 more

1 mention without citation

Dynamic Long-Range Interactions Influence Substrate Binding and Catalysis by Human Histidine Triad Nucleotide-Binding Proteins (HINTs), Key Regulators of Multiple Cellular Processes and Activators of Antiviral ProTides.
Strom et al. (2022)