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8POD

Crystal structure of the kinase domain of ACVR1 (ALK2) in complex with FKBP12 and MU1700

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004675molecular_functiontransmembrane receptor protein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007178biological_processcell surface receptor protein serine/threonine kinase signaling pathway
A0016020cellular_componentmembrane
B0003007biological_processheart morphogenesis
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005160molecular_functiontransforming growth factor beta receptor binding
B0005246molecular_functioncalcium channel regulator activity
B0005515molecular_functionprotein binding
B0005527molecular_functionmacrolide binding
B0005528molecular_functionFK506 binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0006458biological_process'de novo' protein folding
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0014802cellular_componentterminal cisterna
B0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
B0016020cellular_componentmembrane
B0016529cellular_componentsarcoplasmic reticulum
B0016853molecular_functionisomerase activity
B0030018cellular_componentZ disc
B0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
B0030547molecular_functionsignaling receptor inhibitor activity
B0032880biological_processregulation of protein localization
B0032926biological_processnegative regulation of activin receptor signaling pathway
B0033017cellular_componentsarcoplasmic reticulum membrane
B0034713molecular_functiontype I transforming growth factor beta receptor binding
B0042026biological_processprotein refolding
B0042110biological_processT cell activation
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0044325molecular_functiontransmembrane transporter binding
B0050776biological_processregulation of immune response
B0051604biological_processprotein maturation
B0055010biological_processventricular cardiac muscle tissue morphogenesis
B0060347biological_processheart trabecula formation
B0070411molecular_functionI-SMAD binding
B0070697molecular_functionactivin receptor binding
B0097435biological_processsupramolecular fiber organization
B0098562cellular_componentcytoplasmic side of membrane
B1902991biological_processregulation of amyloid precursor protein catabolic process
B1990000biological_processamyloid fibril formation
B1990425cellular_componentryanodine receptor complex
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues22
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGRYGEVWrGswqgen............VAVK
ChainResidueDetails
AVAL214-LYS235

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKskNILV
ChainResidueDetails
AILE332-VAL344

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P26883
ChainResidueDetails
BLYS53

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AVAL214
ALYS235

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 362
ChainResidueDetails
BTYR27electrostatic destabiliser, steric role
BPHE37electrostatic destabiliser, polar/non-polar interaction, steric role
BASP38electrostatic stabiliser, steric role
BILE57electrostatic stabiliser, steric role
BTYR83electrostatic stabiliser, steric role
BPHE100electrostatic destabiliser, polar/non-polar interaction, steric role

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PDB entries from 2025-06-18

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