7MO9
Cryo-EM map of the c-MET II/HGF I/HGF II (K4 and SPH) sub-complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0004713 | molecular_function | protein tyrosine kinase activity |
| E | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| E | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| E | 0016020 | cellular_component | membrane |
| E | 0017154 | molecular_function | semaphorin receptor activity |
| E | 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 | |
| A | TYR259-CYS271 | |
| A | TYR353-CYS365 | |
| A | TYR439-CYS452 |
| site_id | PS00107 |
| Number of Residues | 27 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK |
| Chain | Residue | Details |
| E | ILE1084-LYS1110 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML |
| Chain | Residue | Details |
| E | PHE1200-LEU1212 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 907 |
| Details | TOPO_DOM: Extracellular => ECO:0000255 |
| Chain | Residue | Details |
| E | GLU25-THR932 | |
| D | GLN32 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| E | GLY933-LEU955 | |
| A | ASN402 | |
| A | ASN566 | |
| A | ASN653 | |
| D | ASN294 | |
| D | ASN402 | |
| D | ASN566 | |
| D | ASN653 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 434 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
| Chain | Residue | Details |
| E | LYS956-SER1390 | |
| D | THR476 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
| Chain | Residue | Details |
| E | ASP1204 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| E | ILE1084 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| E | LYS1110 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | SITE: Cleavage => ECO:0000255 |
| Chain | Residue | Details |
| E | ARG307 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | SITE: Required for ligand-induced CBL-mediated ubiquitination => ECO:0000269|PubMed:12244174 |
| Chain | Residue | Details |
| E | TYR1003 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | SITE: Breakpoint for translocation to form TPR-MET oncogene |
| Chain | Residue | Details |
| E | GLU1009 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| E | SER966 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976 |
| Chain | Residue | Details |
| E | THR977 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| E | SER990 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
| Chain | Residue | Details |
| E | SER997 | |
| E | SER1000 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| E | TYR1003 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979 |
| Chain | Residue | Details |
| E | TYR1230 | |
| E | TYR1365 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979 |
| Chain | Residue | Details |
| E | TYR1234 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790 |
| Chain | Residue | Details |
| E | TYR1235 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| E | THR1289 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258 |
| Chain | Residue | Details |
| E | TYR1349 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258 |
| Chain | Residue | Details |
| E | TYR1356 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 10 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| E | ASN45 | |
| E | ASN930 | |
| E | ASN149 | |
| E | ASN202 | |
| E | ASN399 | |
| E | ASN405 | |
| E | ASN607 | |
| E | ASN635 | |
| E | ASN785 | |
| E | ASN879 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19196183 |
| Chain | Residue | Details |
| E | ASN106 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 3 |
| Details | CARBOHYD: O-linked (Man) threonine => ECO:0000269|PubMed:37186866 |
| Chain | Residue | Details |
| E | THR582 | |
| E | THR676 | |
| E | THR761 |
