5TWU
Structure of Maternal Embryonic Leucine Zipper 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. IGTGGFAKVKlAchiltgem..........VAIK |
Chain | Residue | Details |
A | ILE17-LYS40 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKpeNLLF |
Chain | Residue | Details |
A | TYR128-PHE140 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP132 | |
B | ASP132 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | ILE17 | |
A | LYS40 | |
B | ILE17 | |
B | LYS40 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:16216881 |
Chain | Residue | Details |
A | THR56 | |
B | THR56 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16216881 |
Chain | Residue | Details |
A | TYR163 | |
B | TYR163 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:16216881, ECO:0000269|PubMed:16628004 |
Chain | Residue | Details |
A | THR167 | |
B | THR167 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16216881 |
Chain | Residue | Details |
A | SER171 | |
A | SER253 | |
A | SER336 | |
B | SER171 | |
B | SER253 | |
B | SER336 |