Function and Biology Details
Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132674 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Receptor tyrosine-protein kinase erbB-2
Molecule details ›
Chain: A
Length: 44 amino acids
Theoretical weight: 4.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Epidermal growth factor receptor transmembrane-juxtamembrane segment
Structure domains: Cytochrome c1, transmembrane anchor, C-terminal
Length: 44 amino acids
Theoretical weight: 4.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P04626 (Residues: 641-684; Coverage: 4%)
Sequence domains: Epidermal growth factor receptor transmembrane-juxtamembrane segment
Structure domains: Cytochrome c1, transmembrane anchor, C-terminal
Epidermal growth factor receptor
Molecule details ›
Chain: B
Length: 44 amino acids
Theoretical weight: 4.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Epidermal growth factor receptor transmembrane-juxtamembrane segment
Structure domains: Immunoglobulin FC, subunit C
Length: 44 amino acids
Theoretical weight: 4.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P00533 (Residues: 634-677; Coverage: 4%)
Sequence domains: Epidermal growth factor receptor transmembrane-juxtamembrane segment
Structure domains: Immunoglobulin FC, subunit C
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
torsion angle dynamics
Expression system: Escherichia coli
