8ZTC
Crystal structure of Mps1-AMP complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000196 | biological_process | cell integrity MAPK cascade |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004707 | molecular_function | MAP kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0006950 | biological_process | response to stress |
A | 0016301 | molecular_function | kinase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0032995 | biological_process | regulation of fungal-type cell wall biogenesis |
A | 0050850 | biological_process | positive regulation of calcium-mediated signaling |
A | 0051094 | biological_process | positive regulation of developmental process |
A | 1902413 | biological_process | negative regulation of mitotic cytokinesis |
A | 1902660 | biological_process | negative regulation of glucose mediated signaling pathway |
A | 1905665 | biological_process | positive regulation of calcium ion import across plasma membrane |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGAYGIVCaAvnnqtsegv.........AIKK |
Chain | Residue | Details |
A | LEU29-LYS53 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpgNLLV |
Chain | Residue | Details |
A | VAL145-VAL157 |
site_id | PS01351 |
Number of Residues | 104 |
Details | MAPK MAP kinase signature. FskkilakralREikllqhfrghrnitclydmdiprpdnfnetylyeelmecdlaaiirsgqpltdahfqsfiyqilcglkyihsanvlh.........RDlKpgnllvnadC |
Chain | Residue | Details |
A | PHE58-CYS161 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU29 | |
A | LYS52 |