Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CMK

CRYSTAL STRUCTURES OF THE MYRISTYLATED CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE REVEAL OPEN AND CLOSED CONFORMATIONS

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0001669	cellular_component	acrosomal vesicle
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	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	0016310	biological_process	phosphorylation
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	0042585	cellular_component	germinal vesicle
E	0048471	cellular_component	perinuclear region of cytoplasm
E	0106310	molecular_function	protein serine kinase activity
E	1904145	biological_process	negative regulation of meiotic cell cycle process involved in oocyte maturation
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	1
Details	BINDING SITE FOR RESIDUE IOD I 384

Chain	Residue
I	TYR3

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE IOD I 385

Chain	Residue
I	TYR3

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MYR E 0

Chain	Residue
E	TYR306
E	GLY1
E	SER14
E	PHE18
E	PHE100
E	LEU152
E	TYR156
E	ILE303

site_id	AC4
Number of Residues	35
Details	BINDING SITE FOR CHAIN I OF CAMP-DEPENDENT PROTEIN KINASE INHIBITOR, ALPHA FORM

Chain	Residue
E	THR51
E	GLN84
E	HIS87
E	GLU127
E	PHE129
E	ARG133
E	LYS168
E	PRO169
E	GLU170
E	PHE187
E	TPO197
E	LEU198
E	CYS199
E	GLY200
E	THR201
E	PRO202
E	GLU203
E	TYR204
E	GLU230
E	TYR235
E	PHE239
E	ALA240
E	ASP241
E	ASP241
E	ILE246
E	TYR247
E	PRO321
E	GLY322
E	ASN326
E	PHE327
E	ASP328
E	ASP329
E	TYR330
I	IOD384
I	IOD385

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	LEU49-LYS72

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

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	ARG11
I	ARG14
I	ARG15

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
E	GLY50
E	ILE73
E	LEU49
E	LYS72

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
E	TYR122
E	PRO169
E	GLU121
E	LYS168

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

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250\|UniProtKB:P05132

Chain	Residue	Details
E	GLU11
E	SER10

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P17612

Chain	Residue	Details
E	LEU49
E	TRP196
E	THR48
E	THR195

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P05132

Chain	Residue	Details
E	GLU140
E	SER139

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

Chain	Residue	Details
E	LEU198

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P05132

Chain	Residue	Details
E	GLU331
E	TYR330

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

Chain	Residue	Details
E	ILE339

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

Chain	Residue	Details
E	ASN2

site_id	SWS_FT_FI12
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10027

Chain	Residue	Details
E	ASP166

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Deamidated asparagine; partial => ECO:0000269\|PubMed:10684253, ECO:0000269\|PubMed:9521123

Chain	Residue	Details
E	ASN2

site_id	SWS_FT_FI14
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000250\|UniProtKB:P00517

Chain	Residue	Details
E	TPO197

site_id	SWS_FT_FI15
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P00517

Chain	Residue	Details
E	SEP338

site_id	SWS_FT_FI16
Number of Residues	1
Details	LIPID: N-myristoyl glycine => ECO:0000269\|PubMed:9521123

Chain	Residue	Details
E	GLY1

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	GLU170
E	ASP166

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	ASP166
E	LYS168

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	THR201
E	ASP166
E	LYS168

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
E	ASP166
E	ASN171
E	LYS168

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)