Structure of PDB 3my0 Chain X

Receptor sequence
>3my0X (length=257) Species: 9606 (Homo sapiens) [Search protein sequence]
QRTVARQVALVECVGKGRYGEVWRGLWHGESVAVKIFSSRDEQSWFRETE
IYNTVLLRHDNILGFIASDMTLWLITHYHEHGSLYDFLQRQTLEPHLALR
LAVSAACGLAHLHVEIKPAIAHRDFKSRNVLVKSNLQCCIADLGLAVMNN
PRVGTKRYMAPEVLDEQIRTDCFESYKWTDIWAFGLVLWEIARREDYRPP
FYDVVPNDPSFEDMKKVVCVDQQTPTIPNRLALAQMMRECWYPNPSARLT
ALRIKKT
3D structure
PDB3my0 A small molecule targeting ALK1 prevents Notch cooperativity and inhibits functional angiogenesis.
ChainX
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D330 R334
Catalytic site (residue number reindexed from 1) D124 R128
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 LDN X A227 K229 H280 E281 H282 G283 D287 N335 L337 A347 A33 K35 H79 E80 H81 G82 D86 N129 L131 A141 BindingDB: IC50=2.0nM
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:3my0, PDBe:3my0, PDBj:3my0
PDBsum3my0
PubMed25557927
UniProtP37023|ACVL1_HUMAN Serine/threonine-protein kinase receptor R3 (Gene Name=ACVRL1)

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