› 3rcd

X-ray diffraction
3.21Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-138062 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor tyrosine-protein kinase erbB-2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 338 amino acids
Theoretical weight: 38.23 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P04626 (Residues: 713-1028; Coverage: 26%)
Gene names: ERBB2, HER2, MLN19, NEU, NGL
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 03P 2 x 03P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P1
Unit cell:
a: 50.542Å b: 64.936Å c: 92.36Å
α: 90.42° β: 89.72° γ: 90.35°
R-values:
R R work R free
0.227 0.224 0.294
Expression system: Spodoptera frugiperda

Quick links

Citations

7 review citations

αC helix displacement as a general approach for allosteric modulation of protein kinases.
Palmieri et al. (2013)
6 more

52 mentions without citation

Exploring the chemotherapeutic potential of currently used kinase inhibitors: An update.
Naik et al. (2022)
51 more