5VIL

Crystal structure of ASK1 kinase domain with a potent inhibitor (analog 6)

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
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue 9E1 A 1001

Chain	Residue
A	LEU686
A	VAL757
A	PRO758
A	GLY759
A	GLY760
A	ASP807
A	LEU810
A	SER821
A	ASP822
A	DMS1002
B	TYR814
A	LYS688
A	GLY689
A	ALA707
A	LYS709
A	VAL738
A	MET754
A	GLU755
A	GLN756

---

site_id	AC2
Number of Residues	4
Details	binding site for residue DMS A 1002

Chain	Residue
A	TYR814
A	9E11001
B	TYR814
B	DMS1004

---

site_id	AC3
Number of Residues	18
Details	binding site for residue 9E1 B 1001

Chain	Residue
A	TYR814
B	LEU686
B	GLY689
B	ALA707
B	LYS709
B	VAL738
B	GLU755
B	GLN756
B	VAL757
B	PRO758
B	GLY759
B	GLY760
B	ASP807
B	ASN808
B	LEU810
B	SER821
B	ASP822
B	DMS1004

---

site_id	AC4
Number of Residues	4
Details	binding site for residue DMS B 1002

Chain	Residue
A	GLU676
A	GLN703
B	LYS769
B	TRP770

---

site_id	AC5
Number of Residues	7
Details	binding site for residue DMS B 1003

Chain	Residue
A	LYS769
A	TRP770
B	GLU676
B	ARG698
B	GLN703
B	ARG705
B	HOH1108

---

site_id	AC6
Number of Residues	3
Details	binding site for residue DMS B 1004

Chain	Residue
A	DMS1002
B	TYR814
B	9E11001

---

site_id	AC7
Number of Residues	17
Details	binding site for residue 9E1 C 4000

Chain	Residue
C	LEU686
C	GLY689
C	ALA707
C	LYS709
C	VAL738
C	MET754
C	GLU755
C	GLN756
C	VAL757
C	PRO758
C	GLY759
C	GLY760
C	ASP807
C	ASN808
C	LEU810
C	ASP822
D	TYR814

---

site_id	AC8
Number of Residues	15
Details	binding site for residue 9E1 D 4000

Chain	Residue
C	TYR814
D	LEU686
D	ALA707
D	LYS709
D	VAL738
D	MET754
D	GLU755
D	GLN756
D	VAL757
D	PRO758
D	GLY759
D	GLY760
D	ASP807
D	LEU810
D	ASP822

---

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	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP803
B	ASP803
C	ASP803
D	ASP803

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU686
B	LEU686
C	LEU686
D	LEU686

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	LYS709
B	LYS709
C	LYS709
D	LYS709

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:16407264

Chain	Residue	Details
A	TYR718
B	TYR718
C	TYR718
D	TYR718

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17937911

Chain	Residue	Details
A	THR813
A	THR842
B	THR813
B	THR842
C	THR813
C	THR842
D	THR813
D	THR842

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis, MELK and MAP3K6 => ECO:0000269|PubMed:11920685, ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:17937911, ECO:0000269|PubMed:18948261, ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:23102700

Chain	Residue	Details
A	THR838
B	THR838
C	THR838
D	THR838

---