1SZM
DUAL BINDING MODE OF BISINDOLYLMALEIMIDE 2 TO PROTEIN KINASE A (PKA)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001669 | cellular_component | acrosomal vesicle |
| A | 0001707 | biological_process | mesoderm formation |
| 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 | 0005515 | molecular_function | protein binding |
| 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 | 0016020 | cellular_component | membrane |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0018105 | biological_process | peptidyl-serine phosphorylation |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0031594 | cellular_component | neuromuscular junction |
| 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 | 0048471 | cellular_component | perinuclear region of cytoplasm |
| A | 0106310 | molecular_function | protein serine kinase activity |
| A | 1904262 | biological_process | negative regulation of TORC1 signaling |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0001669 | cellular_component | acrosomal vesicle |
| B | 0001707 | biological_process | mesoderm formation |
| 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 | 0005515 | molecular_function | protein binding |
| 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 | 0016020 | cellular_component | membrane |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0018105 | biological_process | peptidyl-serine phosphorylation |
| B | 0019904 | molecular_function | protein domain specific binding |
| B | 0031594 | cellular_component | neuromuscular junction |
| 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 | 0048471 | cellular_component | perinuclear region of cytoplasm |
| B | 0106310 | molecular_function | protein serine kinase activity |
| B | 1904262 | biological_process | negative regulation of TORC1 signaling |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE BI4 A 351 |
| Chain | Residue |
| A | LEU49 |
| A | ASN171 |
| A | MET173 |
| A | THR183 |
| A | ASP184 |
| A | PHE54 |
| A | ALA70 |
| A | VAL104 |
| A | MET120 |
| A | GLU121 |
| A | TYR122 |
| A | ALA123 |
| A | GLU170 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BI4 B 351 |
| Chain | Residue |
| B | LEU49 |
| B | THR51 |
| B | VAL57 |
| B | ALA70 |
| B | MET120 |
| B | GLU121 |
| B | TYR122 |
| B | ALA123 |
| B | PRO124 |
| B | GLY125 |
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 |
| A | LEU49-LYS72 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLMI |
| Chain | Residue | Details |
| A | LEU162-ILE174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:6286662 |
| Chain | Residue | Details |
| A | LEU167 | |
| B | LEU167 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY50 | |
| A | ILE73 | |
| B | GLY50 | |
| B | ILE73 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | TYR122 | |
| A | PRO169 | |
| B | TYR122 | |
| B | PRO169 |
| 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 | 2 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | GLU11 | |
| B | GLU11 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17612 |
| Chain | Residue | Details |
| A | LEU49 | |
| A | TRP196 | |
| B | LEU49 | |
| B | TRP196 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | GLU140 | |
| B | GLU140 |
| 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 | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | GLU331 | |
| B | GLU331 |
| 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 |
Catalytic Information from CSA
| 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 |
