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7MOB

Cryo-EM structure of 2:2 c-MET/NK1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
C0004672molecular_functionprotein kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
C0016020cellular_componentmembrane
C0017154molecular_functionsemaphorin receptor activity
C0071526biological_processsemaphorin-plexin signaling pathway
D0004672molecular_functionprotein kinase activity
D0004713molecular_functionprotein tyrosine kinase activity
D0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
D0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
D0016020cellular_componentmembrane
D0017154molecular_functionsemaphorin receptor activity
D0071526biological_processsemaphorin-plexin signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. YCRNprgeeggpWC
ChainResidueDetails
ATYR176-CYS189

site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK
ChainResidueDetails
CILE1084-LYS1110

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML
ChainResidueDetails
CPHE1200-LEU1212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues172
DetailsDomain: {"description":"PAN","evidences":[{"source":"PROSITE-ProRule","id":"PRU00315","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues156
DetailsDomain: {"description":"Kringle 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19196183","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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