4YZD

Crystal Structure of human phosphorylated IRE1alpha in complex with ADP-Mg

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	3
Details	binding site for residue MG A 1001

Chain	Residue
A	ASN693
A	ASP711
A	ADP1002

---

site_id	AC2
Number of Residues	16
Details	binding site for residue ADP A 1002

Chain	Residue
A	GLU643
A	CYS645
A	THR648
A	LYS690
A	HIS692
A	ASN693
A	LEU695
A	ASP711
A	MG1001
A	HOH1106
A	HIS579
A	GLY580
A	THR584
A	ALA597
A	LYS599
A	ILE642

---

site_id	AC3
Number of Residues	4
Details	binding site for residue MG B 1001

Chain	Residue
B	HIS692
B	ASN693
B	ASP711
B	ADP1002

---

site_id	AC4
Number of Residues	15
Details	binding site for residue ADP B 1002

Chain	Residue
B	GLY580
B	THR584
B	VAL586
B	ALA597
B	LYS599
B	ILE642
B	GLU643
B	CYS645
B	THR648
B	LYS690
B	HIS692
B	ASN693
B	LEU695
B	ASP711
B	MG1001

---

site_id	AC5
Number of Residues	13
Details	binding site for residue ADP C 1001

Chain	Residue
C	GLY578
C	HIS579
C	GLY580
C	VAL586
C	ALA597
C	LYS599
C	ILE642
C	GLU643
C	CYS645
C	THR648
C	LYS690
C	HIS692
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

---