1CDK
CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (E.C.2.7.1.37) (PROTEIN KINASE A) COMPLEXED WITH PROTEIN KINASE INHIBITOR PEPTIDE FRAGMENT 5-24 (PKI(5-24) ISOELECTRIC VARIANT CA) AND MN2+ ADENYLYL IMIDODIPHOSPHATE (MNAMP-PNP) AT PH 5.6 AND 7C AND 4C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001669 | cellular_component | acrosomal vesicle |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004679 | molecular_function | AMP-activated protein kinase activity |
| A | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0010737 | biological_process | protein kinase A signaling |
| A | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0036126 | cellular_component | sperm flagellum |
| A | 0042585 | cellular_component | germinal vesicle |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1904145 | biological_process | negative regulation of meiotic cell cycle process involved in oocyte maturation |
| A | 1904262 | biological_process | negative regulation of TORC1 signaling |
| B | 0001669 | cellular_component | acrosomal vesicle |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004679 | molecular_function | AMP-activated protein kinase activity |
| B | 0004691 | molecular_function | cAMP-dependent protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005952 | cellular_component | cAMP-dependent protein kinase complex |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0010737 | biological_process | protein kinase A signaling |
| B | 0034237 | molecular_function | protein kinase A regulatory subunit binding |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0036126 | cellular_component | sperm flagellum |
| B | 0042585 | cellular_component | germinal vesicle |
| B | 0048471 | cellular_component | perinuclear region of cytoplasm |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 1904145 | biological_process | negative regulation of meiotic cell cycle process involved in oocyte maturation |
| B | 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 |
| J | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
| J | 0006469 | biological_process | negative regulation of protein kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 401 |
| Chain | Residue |
| A | ASN171 |
| A | ASP184 |
| A | ANP400 |
| A | HOH451 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 402 |
| Chain | Residue |
| A | ASP184 |
| A | ANP400 |
| A | HOH436 |
| A | HOH514 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ANP A 400 |
| Chain | Residue |
| A | SER53 |
| A | PHE54 |
| A | GLY55 |
| A | VAL57 |
| A | ALA70 |
| A | LYS72 |
| A | VAL104 |
| A | MET120 |
| A | GLU121 |
| A | VAL123 |
| A | GLU127 |
| A | ASP166 |
| A | LYS168 |
| A | GLU170 |
| A | ASN171 |
| A | LEU173 |
| A | THR183 |
| A | ASP184 |
| A | MN401 |
| A | MN402 |
| A | HOH436 |
| A | HOH451 |
| I | ARG14 |
| I | ALA17 |
| A | GLY52 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MYR A 403 |
| Chain | Residue |
| A | PHE18 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 401 |
| Chain | Residue |
| B | ASN171 |
| B | ASP184 |
| B | ANP400 |
| B | HOH449 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 402 |
| Chain | Residue |
| B | ASP184 |
| B | ANP400 |
| B | HOH435 |
| B | HOH506 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ANP B 400 |
| Chain | Residue |
| B | THR51 |
| B | GLY52 |
| B | SER53 |
| B | PHE54 |
| B | GLY55 |
| B | VAL57 |
| B | ALA70 |
| B | LYS72 |
| B | VAL104 |
| B | MET120 |
| B | GLU121 |
| B | VAL123 |
| B | GLU127 |
| B | ASP166 |
| B | LYS168 |
| B | GLU170 |
| B | ASN171 |
| B | LEU173 |
| B | THR183 |
| B | ASP184 |
| B | PHE327 |
| B | MN401 |
| B | MN402 |
| B | HOH449 |
| J | ARG14 |
| J | ALA17 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MYR B 403 |
| Chain | Residue |
| B | LEU152 |
| B | GLU155 |
| site_id | AC9 |
| Number of Residues | 54 |
| Details | BINDING SITE FOR CHAIN I OF PROTEIN KINASE INHIBITOR |
| Chain | Residue |
| A | TYR330 |
| A | GLU349 |
| A | ANP400 |
| A | HOH411 |
| A | HOH440 |
| A | HOH453 |
| A | HOH500 |
| A | HOH507 |
| A | HOH526 |
| A | HOH532 |
| I | HOH49 |
| I | HOH54 |
| I | HOH63 |
| I | HOH73 |
| I | HOH75 |
| I | HOH76 |
| I | HOH77 |
| I | HOH79 |
| I | HOH88 |
| I | HOH110 |
| I | HOH111 |
| I | HOH129 |
| I | HOH146 |
| I | HOH147 |
| I | HOH148 |
| A | THR51 |
| A | GLY52 |
| A | SER53 |
| A | PHE54 |
| A | LEU82 |
| A | GLU86 |
| A | LEU89 |
| A | ARG93 |
| A | GLU127 |
| A | PHE129 |
| A | ARG133 |
| A | LYS168 |
| A | PRO169 |
| A | GLU170 |
| A | PHE187 |
| A | LYS189 |
| A | ARG190 |
| A | VAL191 |
| A | LYS192 |
| A | LEU198 |
| A | GLY200 |
| A | THR201 |
| A | PRO202 |
| A | GLU203 |
| A | GLU230 |
| A | TYR235 |
| A | PHE239 |
| A | ALA240 |
| A | ASP241 |
| site_id | BC1 |
| Number of Residues | 52 |
| Details | BINDING SITE FOR CHAIN J OF PROTEIN KINASE INHIBITOR |
| Chain | Residue |
| B | THR51 |
| B | GLY52 |
| B | SER53 |
| B | PHE54 |
| B | GLU86 |
| B | LEU89 |
| B | ARG93 |
| B | GLU127 |
| B | PHE129 |
| B | ARG133 |
| B | LYS168 |
| B | PRO169 |
| B | GLU170 |
| B | ARG190 |
| B | VAL191 |
| B | LYS192 |
| B | GLY200 |
| B | THR201 |
| B | PRO202 |
| B | GLU203 |
| B | GLU230 |
| B | GLY234 |
| B | TYR235 |
| B | PRO236 |
| B | PHE239 |
| B | ALA240 |
| B | ASP241 |
| B | ILE246 |
| B | TYR330 |
| B | GLU349 |
| B | ANP400 |
| B | HOH412 |
| B | HOH451 |
| B | HOH456 |
| B | HOH500 |
| B | HOH527 |
| J | HOH196 |
| J | HOH210 |
| J | HOH211 |
| J | HOH218 |
| J | HOH221 |
| J | HOH222 |
| J | HOH223 |
| J | HOH224 |
| J | HOH225 |
| J | HOH254 |
| J | HOH256 |
| J | HOH257 |
| J | HOH258 |
| J | HOH288 |
| J | HOH296 |
| J | HOH312 |
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 |
| A | LEU49-LYS72 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI |
| Chain | Residue | Details |
| A | LEU162-ILE174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | SITE: Important for inhibition |
| Chain | Residue | Details |
| I | ARG11 | |
| I | ARG14 | |
| I | ARG15 | |
| J | ARG11 | |
| J | ARG14 | |
| J | ARG15 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY50 | |
| A | ILE73 | |
| B | GLY50 | |
| B | ILE73 | |
| A | LEU49 | |
| A | LYS72 | |
| B | LEU49 | |
| B | LYS72 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | TYR122 | |
| A | PRO169 | |
| B | TYR122 | |
| B | PRO169 | |
| A | GLU121 | |
| A | LYS168 | |
| B | GLU121 | |
| B | LYS168 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:11152138, ECO:0000269|PubMed:9521123 |
| Chain | Residue | Details |
| A | ALA3 | |
| B | ALA3 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | GLU11 | |
| B | GLU11 | |
| A | SER10 | |
| B | SER10 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612 |
| Chain | Residue | Details |
| A | LEU49 | |
| A | TRP196 | |
| B | LEU49 | |
| B | TRP196 | |
| A | THR48 | |
| A | THR195 | |
| B | THR48 | |
| B | THR195 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | GLU140 | |
| B | GLU140 | |
| A | SER139 | |
| B | SER139 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | LEU198 | |
| B | LEU198 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | GLU331 | |
| B | GLU331 | |
| A | TYR330 | |
| B | TYR330 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | ILE339 | |
| B | ILE339 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:6262777 |
| Chain | Residue | Details |
| A | ASN2 | |
| B | ASN2 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP166 | |
| B | ASP166 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Deamidated asparagine; partial => ECO:0000269|PubMed:10684253, ECO:0000269|PubMed:9521123 |
| Chain | Residue | Details |
| A | ASN2 | |
| B | ASN2 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517 |
| Chain | Residue | Details |
| A | TPO197 | |
| B | TPO197 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00517 |
| Chain | Residue | Details |
| A | SER338 | |
| B | SER338 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:9521123 |
| Chain | Residue | Details |
| A | GLY1 | |
| B | GLY1 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | GLU170 | |
| A | ASP166 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | GLU170 | |
| B | ASP166 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP166 | |
| A | LYS168 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP166 | |
| B | LYS168 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR201 | |
| A | ASP166 | |
| A | LYS168 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR201 | |
| B | ASP166 | |
| B | LYS168 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP166 | |
| A | ASN171 | |
| A | LYS168 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP166 | |
| B | ASN171 | |
| B | LYS168 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 757 |
| Chain | Residue | Details |
| A | LEU167 | activator, proton acceptor, proton donor |
| A | PRO169 | electrostatic stabiliser, polar interaction |
| A | LEU172 | metal ligand |
| A | PHE185 | metal ligand |
| A | PRO202 | electrostatic stabiliser, polar interaction |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 757 |
| Chain | Residue | Details |
| B | LEU167 | activator, proton acceptor, proton donor |
| B | PRO169 | electrostatic stabiliser, polar interaction |
| B | LEU172 | metal ligand |
| B | PHE185 | metal ligand |
| B | PRO202 | electrostatic stabiliser, polar interaction |
