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7MO8

Cryo-EM structure of 1:1 c-MET I/HGF I complex after focused 3D refinement of 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
Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. YCRNprgeeggpWC
ChainResidueDetails
ATYR176-CYS189
ATYR259-CYS271
ATYR353-CYS365
ATYR439-CYS452

site_idPS00107
Number of Residues27
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK
ChainResidueDetails
BILE1084-LYS1110

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML
ChainResidueDetails
BPHE1200-LEU1212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues907
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
BGLU25-THR932

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BGLY933-LEU955
AASN402
AASN566
AASN653

site_idSWS_FT_FI3
Number of Residues434
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BLYS956-SER1390

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
BASP1204

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BILE1084

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING:
ChainResidueDetails
BLYS1110

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Cleavage => ECO:0000255
ChainResidueDetails
BARG307

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: Required for ligand-induced CBL-mediated ubiquitination => ECO:0000269|PubMed:12244174
ChainResidueDetails
BTYR1003

site_idSWS_FT_FI9
Number of Residues1
DetailsSITE: Breakpoint for translocation to form TPR-MET oncogene
ChainResidueDetails
BGLU1009

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER966

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
BTHR977

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER990

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BSER997
BSER1000

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
BTYR1003

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979
ChainResidueDetails
BTYR1230
BTYR1365

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979
ChainResidueDetails
BTYR1234

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790
ChainResidueDetails
BTYR1235

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BTHR1289

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258
ChainResidueDetails
BTYR1349

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258
ChainResidueDetails
BTYR1356

site_idSWS_FT_FI21
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN45
BASN930
BASN149
BASN202
BASN399
BASN405
BASN607
BASN635
BASN785
BASN879

site_idSWS_FT_FI22
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19196183
ChainResidueDetails
BASN106

site_idSWS_FT_FI23
Number of Residues3
DetailsCARBOHYD: O-linked (Man) threonine => ECO:0000269|PubMed:37186866
ChainResidueDetails
BTHR582
BTHR676
BTHR761

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PDB entries from 2024-07-17

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