1YDR

STRUCTURE OF CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH H7 PROTEIN KINASE INHIBITOR 1-(5-ISOQUINOLINESULFONYL)-2-METHYLPIPERAZINE

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0000166	molecular_function	nucleotide binding
E	0001669	cellular_component	acrosomal vesicle
E	0001707	biological_process	mesoderm formation
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0004679	molecular_function	AMP-activated protein kinase activity
E	0004691	molecular_function	cAMP-dependent protein kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005739	cellular_component	mitochondrion
E	0005829	cellular_component	cytosol
E	0005886	cellular_component	plasma membrane
E	0005952	cellular_component	cAMP-dependent protein kinase complex
E	0006468	biological_process	protein phosphorylation
E	0010737	biological_process	protein kinase A signaling
E	0016020	cellular_component	membrane
E	0016301	molecular_function	kinase activity
E	0016310	biological_process	phosphorylation
E	0016740	molecular_function	transferase activity
E	0018105	biological_process	peptidyl-serine phosphorylation
E	0019904	molecular_function	protein domain specific binding
E	0031594	cellular_component	neuromuscular junction
E	0034237	molecular_function	protein kinase A regulatory subunit binding
E	0034605	biological_process	cellular response to heat
E	0036126	cellular_component	sperm flagellum
E	0048471	cellular_component	perinuclear region of cytoplasm
E	0106310	molecular_function	protein serine kinase activity
E	1904262	biological_process	negative regulation of TORC1 signaling
I	0004862	molecular_function	cAMP-dependent protein kinase inhibitor activity
I	0006469	biological_process	negative regulation of protein kinase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE IQP E 351

Chain	Residue
E	GLY50
E	LEU173
E	THR183
E	PHE327
E	HOH415
E	VAL57
E	ALA70
E	GLU121
E	TYR122
E	VAL123
E	GLU127
E	GLU170
E	ASN171

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK

Chain	Residue	Details
E	LEU49-LYS72

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

Chain	Residue	Details
E	LEU162-ILE174

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	SITE: Important for inhibition => ECO:0000250

Chain	Residue	Details
I	THR16
I	ARG19
I	ASN20

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
E	GLY50
E	ILE73

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
E	TYR122
E	PRO169

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:11152138, ECO:0000269|PubMed:9521123

Chain	Residue	Details
E	ALA3

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132

Chain	Residue	Details
E	GLU11

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612

Chain	Residue	Details
E	LEU49
E	TRP196

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132

Chain	Residue	Details
E	GLU140

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777

Chain	Residue	Details
E	LEU198

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site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132

Chain	Residue	Details
E	GLU331

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site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:6262777

Chain	Residue	Details
E	ILE339

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site_id	SWS_FT_FI11
Number of Residues	1
Details	LIPID: N-myristoyl glycine => ECO:0000269|PubMed:6262777

Chain	Residue	Details
E	ASN2

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 757

Chain	Residue	Details
E	LEU167	activator, proton acceptor, proton donor
E	PRO169	electrostatic stabiliser, polar interaction
E	LEU172	metal ligand
E	PHE185	metal ligand
E	PRO202	electrostatic stabiliser, polar interaction

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