Structure of PDB 4nk9 Chain A

Receptor sequence
>4nk9A (length=281) Species: 9606 (Homo sapiens) [Search protein sequence]
ELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDDKPNRVTKVAVK
MLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYA
SKGNLREYLQARRPPEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAAR
NVLVTEDNVMKIADFGIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVW
SFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMR
DCWHAVPSQRPTFKQLVEDLDRIVALTSNQE
3D structure
PDB4nk9 FGFR1 Kinase Inhibitors: Close Regioisomers Adopt Divergent Binding Modes and Display Distinct Biophysical Signatures.
ChainA
Resolution2.57 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) D146 A148 R150 N151 D164
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 2K5 A L484 G485 G487 V492 A512 K514 E531 I545 V561 A564 G567 L630 D641 F642 L21 G22 G24 V29 A48 K50 E67 I81 V97 A100 G103 L153 D164 F165 PDBbind-CN: -logKd/Ki=8.51,Kd=3.1nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4nk9, PDBe:4nk9, PDBj:4nk9
PDBsum4nk9
PubMed24900792
UniProtP11362|FGFR1_HUMAN Fibroblast growth factor receptor 1 (Gene Name=FGFR1)

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