8GW3
Crystal structure of human TAK1 kinase domain fused with TAB1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 22 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGRGAFGVVCkAkwrakd............VAIK |
| Chain | Residue | Details |
| A | VAL42-LYS63 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiHrDLKppNLLL |
| Chain | Residue | Details |
| A | LEU152-LEU164 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP156 | |
| B | ASP156 | |
| C | ASP156 | |
| D | ASP156 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | VAL42 | |
| B | VAL42 | |
| C | VAL42 | |
| D | VAL42 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS63 | |
| B | LYS63 | |
| C | LYS63 | |
| D | LYS63 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis; alternate => ECO:0000269|PubMed:37832545, ECO:0000305|PubMed:10838074 |
| Chain | Residue | Details |
| A | THR184 | |
| B | THR184 | |
| C | THR184 | |
| D | THR184 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis; alternate => ECO:0000269|PubMed:10838074, ECO:0000269|PubMed:16845370, ECO:0000269|PubMed:19675569, ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:37832545 |
| Chain | Residue | Details |
| A | THR187 | |
| B | THR187 | |
| C | THR187 | |
| D | THR187 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:10702308, ECO:0000269|PubMed:10838074 |
| Chain | Residue | Details |
| A | SER192 | |
| B | SER192 | |
| C | SER192 | |
| D | SER192 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:22406003 |
| Chain | Residue | Details |
| A | LYS72 | |
| B | LYS72 | |
| C | LYS72 | |
| D | LYS72 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q62073 |
| Chain | Residue | Details |
| D | LYS158 | |
| D | LYS209 | |
| A | LYS158 | |
| A | LYS209 | |
| B | LYS158 | |
| B | LYS209 | |
| C | LYS158 | |
| C | LYS209 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | SITE: Required for interaction with MAP3K7 => ECO:0000269|PubMed:11323434 |
| Chain | Residue | Details |
| A | PHE484 | |
| B | PHE484 | |
| C | PHE484 | |
| D | PHE484 |
