9D8F

Crystal structure of the ACVR1 (ALK2) Kinase Domain in complex with inhibitor CDD-2281

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
A	0016020	cellular_component	membrane
B	0004672	molecular_function	protein kinase activity
B	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
B	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	22
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGRYGEVWrGswqgen............VAVK

Chain	Residue	Details
A	VAL214-LYS235

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKskNILV

Chain	Residue	Details
A	ILE332-VAL344

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP336
B	ASP336

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	VAL214
A	LYS235
B	VAL214
B	LYS235

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER501
B	SER501

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