› 5h3q

X-ray diffraction
2.1Å resolution

Crystal Structure of TrkA kinase with ligand

Released:
DOI: 10.2210/pdb5h3q/pdb
PDB entry 5h3q coloured by chain, front view.
PDB entry 5h3q coloured by chain, side view.
PDB entry 5h3q coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The juxtamembrane region of TrkA kinase is critical for inhibitor selectivity.
Furuya N, Momose T, Katsuno K, Fushimi N, Muranaka H, Handa C, Ozawa T, Kinoshita T
Bioorg Med Chem Lett 27 1233-1236 (2017)
PMID: 28159414

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High affinity nerve growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 324 amino acids
Theoretical weight: 36.49 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P04629 (Residues: 473-796; Coverage: 42%)
Gene names: MTC, NTRK1, TRK, TRKA
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 7HF 1 x 7HF
Ligand DTT 2 x DTT
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C222
Unit cell:
a: 140.845Å b: 157.195Å c: 52.306Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.215
Expression system: Trichoplusia ni

Quick links

Citations

3 review citations

Evaluation of Substituted Pyrazole-Based Kinase Inhibitors in One Decade (2011-2020): Current Status and Future Prospects.
El-Gamal et al. (2022)
2 more

2 mentions without citation

Insights into Current Tropomyosin Receptor Kinase (TRK) Inhibitors: Development and Clinical Application.
Yan et al. (2019)
1 more