5EAK
Optimization of Microtubule Affinity Regulating Kinase (MARK) Inhibitors with Improved Physical Properties
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 | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue 24R A 1000 |
| Chain | Residue |
| A | GLY60 |
| A | SER133 |
| A | GLY135 |
| A | GLU179 |
| A | LEU182 |
| A | ASP193 |
| A | SER197 |
| A | LYS61 |
| A | VAL67 |
| A | ALA80 |
| A | LYS82 |
| A | MET129 |
| A | GLU130 |
| A | TYR131 |
| A | ALA132 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue 24R B 1000 |
| Chain | Residue |
| B | LYS61 |
| B | ALA80 |
| B | LYS82 |
| B | MET129 |
| B | GLU130 |
| B | TYR131 |
| B | ALA132 |
| B | SER133 |
| B | GLU179 |
| B | LEU182 |
| B | ASP193 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGNFAKVKlArhiltgke..........VAVK |
| Chain | Residue | Details |
| A | ILE59-LYS82 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKaeNLLL |
| Chain | Residue | Details |
| A | ILE171-LEU183 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9H0K1, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP175 | |
| B | ASP175 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9H0K1, ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ILE59 | |
| B | ILE59 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O08678, ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LYS82 | |
| B | LYS82 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER40 | |
| B | SER40 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:O08679 |
| Chain | Residue | Details |
| A | THR58 | |
| A | THR275 | |
| B | THR58 | |
| B | THR275 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine; by CaMK1 => ECO:0000250|UniProtKB:O08679 |
| Chain | Residue | Details |
| A | SER91 | |
| A | SER92 | |
| A | SER93 | |
| B | SER91 | |
| B | SER92 | |
| B | SER93 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by LKB1 and TAOK1 => ECO:0000269|PubMed:14976552, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| A | THR208 | |
| B | THR208 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by GSK3-beta => ECO:0000250|UniProtKB:O08679 |
| Chain | Residue | Details |
| A | SER212 | |
| B | SER212 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:O08679 |
| Chain | Residue | Details |
| A | SER274 | |
| B | SER274 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by CaMK1 => ECO:0000250|UniProtKB:O08679 |
| Chain | Residue | Details |
| A | THR294 | |
| B | THR294 |
