6C9D
Crystal structure of KA1-autoinhibited MARK1 kinase
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 PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGNFAKVKlArhvltgre..........VAVK |
| Chain | Residue | Details |
| A | ILE66-LYS89 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKaeNLLL |
| Chain | Residue | Details |
| A | ILE178-LEU190 |
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 | ASP182 | |
| B | ASP182 |
| 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 | ILE66 | |
| B | ILE66 |
| 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 | LYS89 | |
| B | LYS89 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:17573348 |
| Chain | Residue | Details |
| A | THR208 | |
| B | THR208 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by LKB1 and TAOK1 => ECO:0000269|PubMed:14976552 |
| Chain | Residue | Details |
| A | GLU215 | |
| B | GLU215 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by GSK3-beta => ECO:0000250|UniProtKB:O08678 |
| Chain | Residue | Details |
| A | SER219 | |
| B | SER219 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8VHJ5 |
| Chain | Residue | Details |
| A | SER681 | |
| B | ARG722 | |
| B | ARG774 | |
| A | LYS689 | |
| A | GLY692 | |
| A | ARG722 | |
| A | ARG774 | |
| B | SER681 | |
| B | LYS689 | |
| B | GLY692 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976 |
| Chain | Residue | Details |
| A | PHE702 | |
| B | PHE702 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08678 |
| Chain | Residue | Details |
| A | VAL743 | |
| B | VAL743 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by PKC/PRKCZ => ECO:0000250 |
| Chain | Residue | Details |
