Structure of PDB 5e92 Chain A

Receptor sequence
>5e92A (length=298) Species: 9606 (Homo sapiens) [Search protein sequence]
ELLPIELDTLVGKGRFAEVYKAKLKFETVAVKIFPYEEYASWKTEKDIFS
DINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWE
DLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCL
CDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLASAMNLENVESFKQT
DVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVASMADNVLADA
GRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEH
3D structure
PDB5e92 Crystal structures of apo and inhibitor-bound TGF beta R2 kinase domain: insights into TGF beta R isoform selectivity.
ChainA
Resolution2.08 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D379 K381 N384 D397 D411 T421
Catalytic site (residue number reindexed from 1) D134 K136 N139 D152 D166 T176
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 ANP A G251 G253 R254 V258 A275 K277 F327 H328 N332 K381 S383 N384 L386 D397 G12 G14 R15 V19 A30 K32 F82 H83 N87 K136 S138 N139 L141 D152
BS02 MG A N384 D397 N139 D152
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:5e92, PDBe:5e92, PDBj:5e92
PDBsum5e92
PubMed27139629
UniProtP37173|TGFR2_HUMAN TGF-beta receptor type-2 (Gene Name=TGFBR2)

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