7JUZ

Crystal Structure of KSR1:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor Selumetinib

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
C	0000165	biological_process	MAPK cascade
C	0000166	molecular_function	nucleotide binding
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0004708	molecular_function	MAP kinase kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005769	cellular_component	early endosome
C	0005770	cellular_component	late endosome
C	0005813	cellular_component	centrosome
C	0005829	cellular_component	cytosol
C	0005925	cellular_component	focal adhesion
C	0006468	biological_process	protein phosphorylation
C	0016020	cellular_component	membrane
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0032872	biological_process	regulation of stress-activated MAPK cascade
C	0090170	biological_process	regulation of Golgi inheritance
C	0106310	molecular_function	protein serine kinase activity
C	2000641	biological_process	regulation of early endosome to late endosome transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue ANP A 901

Chain	Residue
A	ILE619
A	THR693
A	LYS735
A	ASN738
A	PHE740
A	THR749
A	ASP750
A	GLY622
A	VAL627
A	ALA637
A	ARG639
A	THR686
A	SER687
A	PHE688
A	CYS689

---

site_id	AC2
Number of Residues	15
Details	binding site for residue ANP C 401

Chain	Residue
C	LEU74
C	GLY77
C	VAL82
C	LYS97
C	MET143
C	GLU144
C	GLY149
C	SER150
C	GLN153
C	LYS192
C	SER194
C	ASN195
C	LEU197
C	ASP208
C	3EW402

---

site_id	AC3
Number of Residues	14
Details	binding site for residue 3EW C 402

Chain	Residue
C	LYS97
C	LEU118
C	VAL127
C	ILE141
C	MET143
C	ASP208
C	PHE209
C	GLY210
C	VAL211
C	SER212
C	LEU215
C	ILE216
C	ALA220
C	ANP401

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK

Chain	Residue	Details
C	LEU74-LYS97

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKpsNILV

Chain	Residue	Details
C	ILE186-VAL198
A	ILE729-TYR741

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q6VAB6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21441910","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by RAF","evidences":[{"source":"PubMed","id":"8157000","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---