Structure of PDB 6unp Chain A Binding Site BS07

Receptor Information
>6unp Chain A (length=302) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLDNLKLLELIGRGRYGAVYKGSLDERPVAVKVFSFANRQNFINEKNIYR
VPLMEHDNIARFIVGDERVTADGRMEYLLVMEYYPNGSLCKYLSLHTSDW
VSSCRLAHSVTRGLAYLHTELPRGDHYKPAISHRDLNSRNVLVKNDGTCV
ISDFGLSMRLTGNRLVRPEVGTIRYMAPEVLEGAVNLRDCESALKQVDMY
ALGLIYWEIFMRCTDLFPGESVPEYQMAFQTEVGNHPTFEDMQVLVSREK
QRPKFPEAWKENSLAVRSLKETIEDCWGQDAEARLTAQCAEERMAELMMI
WE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain6unp Chain A Residue 609 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6unp Structural basis for ALK2/BMPR2 receptor complex signaling through kinase domain oligomerization.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		G212 R213
Binding residue
(residue number reindexed from 1)		G14 R15
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.11.30: receptor protein serine/threonine kinase.
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:6unp, PDBe:6unp, PDBj:6unp
PDBsum6unp
PubMed34400635
UniProtQ13873|BMPR2_HUMAN Bone morphogenetic protein receptor type-2 (Gene Name=BMPR2)

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