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 |