Structure of PDB 4k33 Chain A Binding Site BS02
Receptor Information
>4k33 Chain A (length=293) Species:
9606
(Homo sapiens) [
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LPADPKWELSRARLTLGKPLGEGAFGQVVMAEAIGIDKDRAAKPVTVAVK
MLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYA
AKGNLREFLRARRPPGLDYSFDTSEQLTFKDLVSCAYQVARGMEYLASQK
CIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKETTNGRLPVKWMA
PEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHR
MDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVT
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
4k33 Chain A Residue 802 [
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Receptor-Ligand Complex Structure
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PDB
4k33
Structural Mimicry of A-Loop Tyrosine Phosphorylation by a Pathogenic FGF Receptor 3 Mutation.
Resolution
2.3405 Å
Binding residue
(original residue number in PDB)
N622 D635
Binding residue
(residue number reindexed from 1)
N160 D173
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
D617 A619 R621 N622 D635 R655
Catalytic site (residue number reindexed from 1)
D155 A157 R159 N160 D173 R193
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:4k33
,
PDBe:4k33
,
PDBj:4k33
PDBsum
4k33
PubMed
23972473
UniProt
P22607
|FGFR3_HUMAN Fibroblast growth factor receptor 3 (Gene Name=FGFR3)
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