› 4uip

X-ray diffraction
2.95Å resolution

The complex structure of extracellular domain of EGFR with Repebody (rAC1).

Released:
DOI: 10.2210/pdb4uip/pdb
PDB entry 4uip coloured by chain, front view.
PDB entry 4uip coloured by chain, side view.
PDB entry 4uip coloured by chain, top view.
Source organisms:
Primary publication:
Enzymatic prenylation and oxime ligation for the synthesis of stable and homogeneous protein-drug conjugates for targeted therapy.
Lee JJ, Choi HJ, Yun M, Kang Y, Jung JE, Ryu Y, Kim TY, Cha YJ, Cho HS, Min JJ, Chung CW, Kim HS
Angew Chem Int Ed Engl 54 12020-4 (2015)
PMID: 26315561

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 domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (3 distinct):
Epidermal growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 618 amino acids
Theoretical weight: 68.59 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P00533 (Residues: 26-637; Coverage: 52%)
Gene names: EGFR, ERBB, ERBB1, HER1
Sequence domains:
Structure domains:
Internalin N-terminal domain-containing protein; LRRNT domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 251 amino acids
Theoretical weight: 28.3 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: E0ACT6 (Residues: 33-98, 104-114, 118-119, 142-146; Coverage: 50%)
  • Canonical: Q4G1L3 (Residues: 55-59, 73-75, 78-101, 107-232; Coverage: 56%)
Gene names: VLRB, inlB
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Unit cell:
a: 66.79Å b: 88.34Å c: 189.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.297
Expression systems:
  • Spodoptera frugiperda
  • Escherichia coli

Quick links

Citations

14 review citations

Recent progress in enzymatic protein labelling techniques and their applications.
Zhang et al. (2018)
13 more

5 mentions without citation

Quercetin conjugated with superparamagnetic iron oxide nanoparticles improves learning and memory better than free quercetin via interacting with proteins involved in LTP.
Amanzadeh et al. (2019)
4 more