4FZA
Crystal structure of MST4-MO25 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0007165 | biological_process | signal transduction |
| A | 0010800 | biological_process | positive regulation of peptidyl-threonine phosphorylation |
| A | 0014823 | biological_process | response to activity |
| A | 0018105 | biological_process | peptidyl-serine phosphorylation |
| A | 0019900 | molecular_function | kinase binding |
| A | 0030018 | cellular_component | Z disc |
| A | 0030295 | molecular_function | protein kinase activator activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0035556 | biological_process | intracellular signal transduction |
| A | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071476 | biological_process | cellular hypotonic response |
| A | 0071902 | biological_process | positive regulation of protein serine/threonine kinase activity |
| A | 0097066 | biological_process | response to thyroid hormone |
| A | 1901017 | biological_process | negative regulation of potassium ion transmembrane transporter activity |
| A | 1901380 | biological_process | negative regulation of potassium ion transmembrane transport |
| A | 1902554 | cellular_component | serine/threonine protein kinase complex |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 0004672 | molecular_function | protein 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 | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | SER34 |
| B | ASP144 |
| B | LYS146 |
| B | PHE179 |
| B | GLY181 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | PHE163 |
| B | GOL303 |
| B | THR83 |
| B | GLU100 |
| B | ALA161 |
| B | ALA162 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| B | VAL38 |
| B | LYS53 |
| B | PHE163 |
| B | GOL302 |
| B | HOH1008 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGEVFkGidnrtqqv..........VAIK |
| Chain | Residue | Details |
| B | ILE30-LYS53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| B | ASP144 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| B | ILE30 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:29232556 |
| Chain | Residue | Details |
| B | LYS53 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15037601, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| B | THR178 |
