Ligand: PE5

Total number of chains: 8
Spatial label Dihedral label Number of Chains Representative
DFGin BLAminus 8 8HV6A
All chains
Pymol session (all) Pymol script (all)
Representatives
Pymol session (repr) Pymol script (repr)
All chains - renumbered by
Uniprot PDB Alignment
Database table as tsv

Family Gene UniprotID PDB Resolution Activity Spatial-Dihedral Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop Phosphorylation Mutation Protein
TYR EGFR EGFR_HUMAN 8HV4A 2.2 Active DFGin‑BLAminus in-in in-in PE5, MWU Allosteric, Type1 696 - 1020 3 None E865A,E866A,K867A Epidermal growth factor receptor
TYR EGFR EGFR_HUMAN 8HV6A 2.2 Active DFGin‑BLAminus in-in in-in PE5, N86 Allosteric, Type1 696 - 1020 0 None E865A,E866A,K867A Epidermal growth factor receptor
TYR EGFR EGFR_HUMAN 8HV7A 2.69 Active DFGin‑BLAminus in-in in-in PE5, N8O Allosteric, Type1 696 - 1019 6 None E865A,E866A,K867A Epidermal growth factor receptor
TYR EGFR EGFR_HUMAN 8HV8A 2.4 Active DFGin‑BLAminus in-in in-in PE5, N99 Allosteric, Type1 696 - 1019 0 None C797S,E865A,E866A,K867A Epidermal growth factor receptor
TYR EGFR EGFR_HUMAN 8HV9A 2.5 Active DFGin‑BLAminus in-in in-in PE5, N9L Allosteric, Type1 696 - 1019 0 None E865A,E866A,K867A Epidermal growth factor receptor
TYR EGFR EGFR_HUMAN 8HV1A 2.4 Active DFGin‑BLAminus in-in in-in PE5, N6N Allosteric, Type1 696 - 1019 0 None E865A,E866A,K867A Epidermal growth factor receptor
TYR EGFR EGFR_HUMAN 8HV3A 2.4 Active DFGin‑BLAminus in-in in-in PE5, MWU Allosteric, Type1 696 - 1020 0 None E865A,E866A,K867A Epidermal growth factor receptor
TYR EGFR EGFR_HUMAN 8HV5A 2.2 Active DFGin‑BLAminus in-in in-in PE5, N7C Allosteric, Type1 696 - 1019 0 None E865A,E866A,K867A Epidermal growth factor receptor

Ligand: PE5

Total number of chains: 8
Spatial label Dihedral label Number of Chains Representative
DFGin BLAminus 8 8HV6A
All chains
Pymol session (all) Pymol script (all)
Representatives
Pymol session (repr) Pymol script (repr)
All chains - renumbered by
Uniprot PDB Alignment
Database table as tsv

Family Gene UniprotID PDB Resolution Activity Spatial-Dihedral Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop Phosphorylation Mutation Protein Organism
TYR EGFR EGFR_HUMAN 8HV4A 2.2 Active DFGin‑BLAminus in-in in-in PE5, MWU Allosteric, Type1 696 - 1020 3 None E865A,E866A,K867A Epidermal growth factor receptor Homo sapiens
TYR EGFR EGFR_HUMAN 8HV6A 2.2 Active DFGin‑BLAminus in-in in-in PE5, N86 Allosteric, Type1 696 - 1020 0 None E865A,E866A,K867A Epidermal growth factor receptor Homo sapiens
TYR EGFR EGFR_HUMAN 8HV7A 2.69 Active DFGin‑BLAminus in-in in-in PE5, N8O Allosteric, Type1 696 - 1019 6 None E865A,E866A,K867A Epidermal growth factor receptor Homo sapiens
TYR EGFR EGFR_HUMAN 8HV8A 2.4 Active DFGin‑BLAminus in-in in-in PE5, N99 Allosteric, Type1 696 - 1019 0 None C797S,E865A,E866A,K867A Epidermal growth factor receptor Homo sapiens
TYR EGFR EGFR_HUMAN 8HV9A 2.5 Active DFGin‑BLAminus in-in in-in PE5, N9L Allosteric, Type1 696 - 1019 0 None E865A,E866A,K867A Epidermal growth factor receptor Homo sapiens
TYR EGFR EGFR_HUMAN 8HV1A 2.4 Active DFGin‑BLAminus in-in in-in PE5, N6N Allosteric, Type1 696 - 1019 0 None E865A,E866A,K867A Epidermal growth factor receptor Homo sapiens
TYR EGFR EGFR_HUMAN 8HV3A 2.4 Active DFGin‑BLAminus in-in in-in PE5, MWU Allosteric, Type1 696 - 1020 0 None E865A,E866A,K867A Epidermal growth factor receptor Homo sapiens
TYR EGFR EGFR_HUMAN 8HV5A 2.2 Active DFGin‑BLAminus in-in in-in PE5, N7C Allosteric, Type1 696 - 1019 0 None E865A,E866A,K867A Epidermal growth factor receptor Homo sapiens

Ligand: PE5

Total number of chains: 0
Spatial label Dihedral label Number of Chains Representative
All chains
Pymol session (all) Pymol script (all)
Representatives
Pymol session (repr) Pymol script (repr)
All chains - renumbered by
Uniprot PDB Alignment
Database table as tsv

Family Gene UniprotID PDB Resolution Activity Spatial-Dihedral Chelix-SaltBridge ActLoopNT-ActLoopCT Ligand Type Residues in structure Unresolved residues in A-loop Phosphorylation Mutation Protein Organism