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	78
Details	Domain: {"description":"Kringle 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	77
Details	Domain: {"description":"Kringle 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	226
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000022","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000024","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000025","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	7
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19196183","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (Man) threonine","evidences":[{"source":"PubMed","id":"37186866","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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