Structure of PDB 5e90 Chain A

Receptor sequence
>5e90A (length=303) Species: 9606 (Homo sapiens) [Search protein sequence]
GHMTIARDIVLQESVGKGRFGEVWRGKWRGEEVAVKIFSSREERSWFREA
EIFQTVMLRHENILGFIAADNKDNGTWTQLWLVTDFHEHGNLFDYLNRYT
VTVEGMIKLALSTASGLAHLHMEIVGTQGKPAIAHRDLKSKNILVKKNGT
CCICDFGLAVRHDSATDTIDIAPNHRVGTKRYMAPEVLDDSINMKHFESF
KRADIYAMGLVFWEIARRCSIGGIHEDYQLPYYDLVPSDPSVEEMRKVVC
EQKLRPNIPNRWQSCEALRVMAKIMRECWYANGAARLTALRIKKTLSQLS
QQE
3D structure
PDB5e90 Crystal structures of apo and inhibitor-bound TGF beta R2 kinase domain: insights into TGF beta R isoform selectivity.
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D333 K335 K337 N338 D351 D366 T375
Catalytic site (residue number reindexed from 1) D137 K139 K141 N142 D155 D170 T179
Enzyme Commision number 2.7.11.30: receptor protein serine/threonine 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 5L4 A V211 G214 A230 K232 L260 F282 H283 G286 N287 L340 D351 V15 G18 A34 K36 L64 F86 H87 G90 N91 L144 D155 PDBbind-CN: -logKd/Ki=7.85,IC50=0.014uM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004675 transmembrane receptor protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0007178 cell surface receptor protein serine/threonine kinase signaling pathway
Cellular Component
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5e90, PDBe:5e90, PDBj:5e90
PDBsum5e90
PubMed27139629
UniProtP36897|TGFR1_HUMAN TGF-beta receptor type-1 (Gene Name=TGFBR1)

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