Structure of PDB 6fng Chain A

Receptor sequence
>6fngA (length=277) Species: 9606 (Homo sapiens) [Search protein sequence]
QAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKKEVPVAIKTLKAGYT
EKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKF
LREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVC
KVSDFGLKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWE
LSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSI
LDKLIRAPDSLKTLADFDPRVSIRLPS
3D structure
PDB6fng NVP-BHG712: Effects of Regioisomers on the Affinity and Selectivity toward the EPHrin Family.
ChainA
Resolution1.038 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D739 A741 R743 N744 D757 P780
Catalytic site (residue number reindexed from 1) D136 A138 R140 N141 D154 P160
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine kinase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 DWT A V627 A644 K646 E663 M667 T692 Y694 M695 L730 Y735 S756 D757 F758 V29 A41 K43 E60 M64 T89 Y91 M92 L127 Y132 S153 D154 F155 MOAD: Kd=73nM
PDBbind-CN: -logKd/Ki=7.14,Kd=73nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6fng, PDBe:6fng, PDBj:6fng
PDBsum6fng
PubMed29928781
UniProtP29317|EPHA2_HUMAN Ephrin type-A receptor 2 (Gene Name=EPHA2)

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