Structure of PDB 5eg3 Chain A Binding Site BS03
Receptor Information
>5eg3 Chain A (length=302) Species:
9606
(Homo sapiens) [
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FELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGIDKDKPKEAVTVA
VKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVA
YASKGNLREYLRARRPPGNRVPEEQMTFKDLVSCTYQLARGMEYLASQKC
IHRDLAARNVLVTENNVMKIADFGLARDINNIDFFKETTNGRLPVKWMAP
EALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRM
DKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDL
SQ
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
5eg3 Chain A Residue 803 [
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Receptor-Ligand Complex Structure
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PDB
5eg3
Two FGF Receptor Kinase Molecules Act in Concert to Recruit and Transphosphorylate Phospholipase C gamma.
Resolution
2.606 Å
Binding residue
(original residue number in PDB)
N631 D644
Binding residue
(residue number reindexed from 1)
N159 D172
Annotation score
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.
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
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Molecular Function
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Biological Process
External links
PDB
RCSB:5eg3
,
PDBe:5eg3
,
PDBj:5eg3
PDBsum
5eg3
PubMed
26687682
UniProt
P21802
|FGFR2_HUMAN Fibroblast growth factor receptor 2 (Gene Name=FGFR2)
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