7MOB
Cryo-EM structure of 2:2 c-MET/NK1 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| C | 0016020 | cellular_component | membrane |
| C | 0017154 | molecular_function | semaphorin receptor activity |
| C | 0071526 | biological_process | semaphorin-plexin signaling pathway |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004713 | molecular_function | protein tyrosine kinase activity |
| D | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| D | 0016020 | cellular_component | membrane |
| D | 0017154 | molecular_function | semaphorin receptor activity |
| D | 0071526 | biological_process | semaphorin-plexin signaling pathway |
Functional Information from PROSITE/UniProt
| site_id | PS00021 |
| Number of Residues | 14 |
| Details | KRINGLE_1 Kringle domain signature. YCRNprgeeggpWC |
| Chain | Residue | Details |
| A | TYR176-CYS189 |
| site_id | PS00107 |
| Number of Residues | 27 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK |
| Chain | Residue | Details |
| C | ILE1084-LYS1110 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML |
| Chain | Residue | Details |
| C | PHE1200-LEU1212 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1814 |
| Details | TOPO_DOM: Extracellular => ECO:0000255 |
| Chain | Residue | Details |
| C | GLU25-THR932 | |
| D | GLU25-THR932 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| C | GLY933-LEU955 | |
| D | GLY933-LEU955 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 868 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| C | LYS956-SER1390 | |
| D | LYS956-SER1390 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
| Chain | Residue | Details |
| C | ASP1204 | |
| D | ASP1204 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| C | ILE1084 | |
| D | ILE1084 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| C | LYS1110 | |
| D | LYS1110 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Cleavage => ECO:0000255 |
| Chain | Residue | Details |
| C | ARG307 | |
| D | ARG307 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Required for ligand-induced CBL-mediated ubiquitination => ECO:0000269|PubMed:12244174 |
| Chain | Residue | Details |
| C | TYR1003 | |
| D | TYR1003 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | SITE: Breakpoint for translocation to form TPR-MET oncogene |
| Chain | Residue | Details |
| C | GLU1009 | |
| D | GLU1009 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| C | SER966 | |
| D | SER966 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976 |
| Chain | Residue | Details |
| C | THR977 | |
| D | THR977 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| C | SER990 | |
| D | SER990 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| C | SER997 | |
| C | SER1000 | |
| D | SER997 | |
| D | SER1000 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| C | TYR1003 | |
| D | TYR1003 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979 |
| Chain | Residue | Details |
| C | TYR1230 | |
| C | TYR1365 | |
| D | TYR1230 | |
| D | TYR1365 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979 |
| Chain | Residue | Details |
| C | TYR1234 | |
| D | TYR1234 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790 |
| Chain | Residue | Details |
| C | TYR1235 | |
| D | TYR1235 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| C | THR1289 | |
| D | THR1289 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258 |
| Chain | Residue | Details |
| C | TYR1349 | |
| D | TYR1349 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258 |
| Chain | Residue | Details |
| C | TYR1356 | |
| D | TYR1356 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 20 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| C | ASN45 | |
| C | ASN930 | |
| D | ASN45 | |
| D | ASN149 | |
| D | ASN202 | |
| D | ASN399 | |
| D | ASN405 | |
| D | ASN607 | |
| D | ASN635 | |
| D | ASN785 | |
| D | ASN879 | |
| C | ASN149 | |
| D | ASN930 | |
| C | ASN202 | |
| C | ASN399 | |
| C | ASN405 | |
| C | ASN607 | |
| C | ASN635 | |
| C | ASN785 | |
| C | ASN879 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19196183 |
| Chain | Residue | Details |
| C | ASN106 | |
| D | ASN106 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 6 |
| Details | CARBOHYD: O-linked (Man) threonine => ECO:0000269|PubMed:37186866 |
| Chain | Residue | Details |
| C | THR582 | |
| C | THR676 | |
| C | THR761 | |
| D | THR582 | |
| D | THR676 | |
| D | THR761 |
