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7MO7

Cryo-EM structure of 2:2 c-MET/HGF holo-complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0016020cellular_componentmembrane
B0017154molecular_functionsemaphorin receptor activity
B0071526biological_processsemaphorin-plexin signaling pathway
D0004252molecular_functionserine-type endopeptidase activity
D0006508biological_processproteolysis
E0004672molecular_functionprotein kinase activity
E0004713molecular_functionprotein tyrosine kinase activity
E0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
E0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
E0016020cellular_componentmembrane
E0017154molecular_functionsemaphorin receptor activity
E0071526biological_processsemaphorin-plexin signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. YCRNprgeeggpWC
ChainResidueDetails
DTYR176-CYS189
DTYR259-CYS271
DTYR353-CYS365
DTYR439-CYS452

site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK
ChainResidueDetails
EILE1084-LYS1110

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML
ChainResidueDetails
EPHE1200-LEU1212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1814
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
EGLU25-THR932
BGLU25-THR932

site_idSWS_FT_FI2
Number of Residues44
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
EGLY933-LEU955
BGLY933-LEU955
DASN566
DASN653
AASN294
AASN402
AASN566
AASN653

site_idSWS_FT_FI3
Number of Residues868
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ELYS956-SER1390
BLYS956-SER1390

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
EASP1204
BASP1204

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
EILE1084
BILE1084

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ELYS1110
BLYS1110

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Cleavage => ECO:0000255
ChainResidueDetails
EARG307
BARG307

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Required for ligand-induced CBL-mediated ubiquitination => ECO:0000269|PubMed:12244174
ChainResidueDetails
ETYR1003
BTYR1003

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Breakpoint for translocation to form TPR-MET oncogene
ChainResidueDetails
EGLU1009
BGLU1009

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ESER966
BSER966

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ETHR977
BTHR977

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ESER990
BSER990

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ESER997
ESER1000
BSER997
BSER1000

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
ETYR1003
BTYR1003

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979
ChainResidueDetails
ETYR1230
ETYR1365
BTYR1230
BTYR1365

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979
ChainResidueDetails
ETYR1234
BTYR1234

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790
ChainResidueDetails
ETYR1235
BTYR1235

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ETHR1289
BTHR1289

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258
ChainResidueDetails
ETYR1349
BTYR1349

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258
ChainResidueDetails
ETYR1356
BTYR1356

site_idSWS_FT_FI21
Number of Residues20
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
EASN45
EASN930
BASN45
BASN149
BASN202
BASN399
BASN405
BASN607
BASN635
BASN785
BASN879
EASN149
BASN930
EASN202
EASN399
EASN405
EASN607
EASN635
EASN785
EASN879

site_idSWS_FT_FI22
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19196183
ChainResidueDetails
EASN106
BASN106

site_idSWS_FT_FI23
Number of Residues6
DetailsCARBOHYD: O-linked (Man) threonine => ECO:0000269|PubMed:37186866
ChainResidueDetails
ETHR582
ETHR676
ETHR761
BTHR582
BTHR676
BTHR761

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PDB entries from 2025-06-11

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