Structure of PDB 4rwl Chain B

Receptor sequence
>4rwlB (length=285) Species: 9606 (Homo sapiens) [Search protein sequence]
AGVSEYELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDPNRVTK
VAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVI
VEYASKGNLREYLQARRPPEQLSSKDLVSCAYQVARGMEYLASKKCIHRD
LAARNVLVTEDNVMKIADFGLIDYYKKTTNGRLPVKWMAPEALFDRIYTH
QSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNEL
YMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQ
3D structure
PDB4rwl Illuminating the Molecular Mechanisms of Tyrosine Kinase Inhibitor Resistance for the FGFR1 Gatekeeper Mutation: The Achilles' Heel of Targeted Therapy.
ChainB
Resolution2.193 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D623 A625 R627 N628 D641
Catalytic site (residue number reindexed from 1) D150 A152 R154 N155 D168
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 3ZC B L484 A512 K514 E531 M535 V561 E562 Y563 A564 L630 D641 F642 L27 A52 K54 E71 M75 V101 E102 Y103 A104 L157 D168 F169 MOAD: Kd=8nM
PDBbind-CN: -logKd/Ki=8.10,Kd=8nM
BindingDB: IC50=18nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005007 fibroblast growth factor receptor 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:4rwl, PDBe:4rwl, PDBj:4rwl
PDBsum4rwl
PubMed25686244
UniProtP11362|FGFR1_HUMAN Fibroblast growth factor receptor 1 (Gene Name=FGFR1)

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