4YZ9

Crystal Structure of human phosphorylated IRE1alpha in complex with a type III kinase inhibitor (GSK2850163A)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004521	molecular_function	RNA endonuclease activity
A	0004540	molecular_function	RNA nuclease activity
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006397	biological_process	mRNA processing
A	0006468	biological_process	protein phosphorylation
A	0030968	biological_process	endoplasmic reticulum unfolded protein response
B	0004521	molecular_function	RNA endonuclease activity
B	0004540	molecular_function	RNA nuclease activity
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006397	biological_process	mRNA processing
B	0006468	biological_process	protein phosphorylation
B	0030968	biological_process	endoplasmic reticulum unfolded protein response
C	0004521	molecular_function	RNA endonuclease activity
C	0004540	molecular_function	RNA nuclease activity
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006397	biological_process	mRNA processing
C	0006468	biological_process	protein phosphorylation
C	0030968	biological_process	endoplasmic reticulum unfolded protein response

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue 4K7 A 1001

Chain	Residue
A	ALA581
A	ILE684
A	VAL685
A	HIS686
A	ASP711
A	THR584
A	LYS599
A	CYS605
A	ALA609
A	GLU612
A	VAL613
A	ILE626
A	LEU679

---

site_id	AC2
Number of Residues	9
Details	binding site for residue 4K7 B 1001

Chain	Residue
B	ALA581
B	THR584
B	LYS599
B	ALA609
B	GLU612
B	ILE626
B	HIS686
B	ARG687
B	ASP711

---

site_id	AC3
Number of Residues	11
Details	binding site for residue 4K7 C 1001

Chain	Residue
C	ALA581
C	THR584
C	LYS599
C	ALA609
C	GLU612
C	VAL613
C	ILE626
C	ILE684
C	VAL685
C	HIS686
C	ASP711

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE684-ILE696

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP688
B	ASP688
C	ASP688

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU577
B	LEU577
C	LEU577

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683, ECO:0007744|PDB:3P23

Chain	Residue	Details
A	LYS599
B	LYS599
C	LYS599

---

site_id	SWS_FT_FI4
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:21317875, ECO:0007744|PDB:3P23

Chain	Residue	Details
A	GLU643
A	LYS690
A	ASP711
B	GLU643
B	LYS690
B	ASP711
C	GLU643
C	LYS690
C	ASP711

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	SITE: Interacts with hydroxy-aryl-aldehyde inhibitors => ECO:0000250|UniProtKB:Q9EQY0

Chain	Residue	Details
A	TYR892
B	TYR892
C	TYR892

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:30118681

Chain	Residue	Details
A	SER724
A	SER729
B	SER724
B	SER729
C	SER724
C	SER729

---