5N23
Protein kinase A mutants as surrogate model for Aurora B with AT9283 inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004862 | molecular_function | cAMP-dependent protein kinase inhibitor activity |
| B | 0006469 | biological_process | negative regulation of protein kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue 35R A 401 |
| Chain | Residue |
| A | LEU49 |
| A | SER130 |
| A | LEU173 |
| A | ASP184 |
| A | PHE327 |
| A | ASP328 |
| A | GLY50 |
| A | ALA70 |
| A | LEU120 |
| A | GLU121 |
| A | TYR122 |
| A | ALA123 |
| A | PRO124 |
| A | GLY126 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........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. LiYrDLKpeNLLI |
| Chain | Residue | Details |
| A | 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 |
| B | ARG15 | |
| B | ARG18 | |
| B | ARG19 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU49 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | GLU121 | |
| A | LYS168 | |
| A | LYS72 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Deamidated asparagine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | ASN2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | SEP10 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976 |
| Chain | Residue | Details |
| A | THR48 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | SEP139 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:12372837 |
| Chain | Residue | Details |
| A | THR195 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12372837, ECO:0000269|PubMed:16765046, ECO:0000269|PubMed:20137943, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:20732331, ECO:0000269|PubMed:21774789, ECO:0000269|Ref.43 |
| Chain | Residue | Details |
| A | TPO197 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P05132 |
| Chain | Residue | Details |
| A | TYR330 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16765046, ECO:0000269|PubMed:20137943, ECO:0000269|PubMed:20481595, ECO:0000269|PubMed:20732331, ECO:0000269|PubMed:21774789, ECO:0000269|Ref.43, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SEP338 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | LIPID: N-myristoyl glycine => ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930 |
| Chain | Residue | Details |
| A | GLY1 |
