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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
ChainGOidnamespacecontents
E0001669cellular_componentacrosomal vesicle
E0001707biological_processmesoderm formation
E0004672molecular_functionprotein kinase activity
E0004674molecular_functionprotein serine/threonine kinase activity
E0004679molecular_functionAMP-activated protein kinase activity
E0004691molecular_functioncAMP-dependent protein kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005739cellular_componentmitochondrion
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0005952cellular_componentcAMP-dependent protein kinase complex
E0006468biological_processprotein phosphorylation
E0010737biological_processprotein kinase A signaling
E0016310biological_processphosphorylation
E0018105biological_processpeptidyl-serine phosphorylation
E0019904molecular_functionprotein domain specific binding
E0031594cellular_componentneuromuscular junction
E0034237molecular_functionprotein kinase A regulatory subunit binding
E0034605biological_processcellular response to heat
E0036126cellular_componentsperm flagellum
E0048471cellular_componentperinuclear region of cytoplasm
E0106310molecular_functionprotein serine kinase activity
E1904262biological_processnegative regulation of TORC1 signaling
I0004862molecular_functioncAMP-dependent protein kinase inhibitor activity
I0006469biological_processnegative regulation of protein kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE IQP E 351
ChainResidue
EGLY50
ELEU173
ETHR183
EPHE327
EHOH415
EVAL57
EALA70
EGLU121
ETYR122
EVAL123
EGLU127
EGLU170
EASN171

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhmetgnh..........YAMK
ChainResidueDetails
ELEU49-LYS72

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI
ChainResidueDetails
ELEU162-ILE174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Important for inhibition => ECO:0000250
ChainResidueDetails
ITHR16
IARG19
IASN20

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
EGLY50
EILE73

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ETYR122
EPRO169

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:11152138, ECO:0000269|PubMed:9521123
ChainResidueDetails
EALA3

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
EGLU11

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612
ChainResidueDetails
ELEU49
ETRP196

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
EGLU140

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777
ChainResidueDetails
ELEU198

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132
ChainResidueDetails
EGLU331

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:6262777
ChainResidueDetails
EILE339

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:6262777
ChainResidueDetails
EASN2

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EGLU170
EASP166

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASP166
ELYS168

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ETHR201
EASP166
ELYS168

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
EASP166
EASN171
ELYS168

site_idMCSA1
Number of Residues5
DetailsM-CSA 757
ChainResidueDetails
ELEU167activator, proton acceptor, proton donor
EPRO169electrostatic stabiliser, polar interaction
ELEU172metal ligand
EPHE185metal ligand
EPRO202electrostatic stabiliser, polar interaction

226707

PDB entries from 2024-10-30

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