Structure of PDB 5eg3 Chain A

Receptor sequence
>5eg3A (length=302) Species: 9606 (Homo sapiens) [Search protein sequence]
FELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGIDKDKPKEAVTVA
VKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVA
YASKGNLREYLRARRPPGNRVPEEQMTFKDLVSCTYQLARGMEYLASQKC
IHRDLAARNVLVTENNVMKIADFGLARDINNIDFFKETTNGRLPVKWMAP
EALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRM
DKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDL
SQ
3D structure
PDB5eg3 Two FGF Receptor Kinase Molecules Act in Concert to Recruit and Transphosphorylate Phospholipase C gamma.
ChainA
Resolution2.606 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D626 A628 R630 N631 D644
Catalytic site (residue number reindexed from 1) D154 A156 R158 N159 D172
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 ACP A L487 V495 A515 K517 A567 N571 L633 D644 L22 V30 A50 K52 A102 N106 L161 D172
BS02 MG A R630 N631 R158 N159
BS03 MG A N631 D644 N159 D172
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:5eg3, PDBe:5eg3, PDBj:5eg3
PDBsum5eg3
PubMed26687682
UniProtP21802|FGFR2_HUMAN Fibroblast growth factor receptor 2 (Gene Name=FGFR2)

[Back to BioLiP]