5VIO

Crystal structure of ASK1 kinase domain with a potent inhibitor (analog 13)

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	16
Details	binding site for residue 9E4 A 4000

Chain	Residue
A	LEU686
A	GLY759
A	ASP807
A	LEU810
A	SER821
A	ASP822
A	HOH4105
B	TYR814
A	LYS688
A	GLY689
A	VAL694
A	ALA707
A	LYS709
A	GLU755
A	GLN756
A	VAL757

---

site_id	AC2
Number of Residues	13
Details	binding site for residue 9E4 B 4000

Chain	Residue
A	TYR814
B	LEU686
B	GLY689
B	ALA707
B	LYS709
B	GLU755
B	GLN756
B	VAL757
B	GLY759
B	ASP807
B	LEU810
B	SER821
B	ASP822

---

site_id	AC3
Number of Residues	12
Details	binding site for residue 9E4 D 4000

Chain	Residue
C	TYR814
D	LEU686
D	GLY689
D	ALA707
D	LYS709
D	GLU755
D	GLN756
D	VAL757
D	GLY759
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

---