7MU7

Ask1 bound to compound 3

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
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue DMS A 1001

Chain	Residue
A	TYR673
A	TYR675
A	GLU746

---

site_id	AC2
Number of Residues	1
Details	binding site for residue EDO A 1002

Chain	Residue
A	CYS928

---

site_id	AC3
Number of Residues	14
Details	binding site for residue RFG A 1003

Chain	Residue
A	GLU755
A	GLN756
A	VAL757
A	GLY759
A	ASP807
A	ASN808
A	LEU810
A	ASP822
A	HOH1115
A	LEU686
A	ALA707
A	LYS709
A	VAL738
A	MET754

---

site_id	AC4
Number of Residues	2
Details	binding site for residue EDO B 1001

Chain	Residue
B	TYR673
B	GLU746

---

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO B 1002

Chain	Residue
B	ASP775
B	ASN776
B	GLU777
B	GLN778

---

site_id	AC6
Number of Residues	16
Details	binding site for residue RFG B 1003

Chain	Residue
B	LEU686
B	ALA707
B	LYS709
B	VAL738
B	MET754
B	GLU755
B	GLN756
B	VAL757
B	GLY759
B	GLY760
B	ASP807
B	LEU810
B	SER821
B	ASP822
B	HOH1109
B	HOH1116

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU686-LYS709

---

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

Chain	Residue	Details
A	ILE799-ILE811

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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_FI2
Number of Residues	16
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: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"16407264","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17937911","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis, MELK and MAP3K6","evidences":[{"source":"PubMed","id":"11920685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17210579","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17937911","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18948261","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19590015","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23102700","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---