4U6R

Crystal structure of human IRE1 cytoplasmic domains in complex with a sulfonamide inhibitor.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue 3E4 A 1001

Chain	Residue
A	VAL586
A	GLU651
A	SER710
A	ASP711
A	PHE712
A	LYS851
A	HOH1130
A	ALA597
A	LYS599
A	GLU612
A	LEU616
A	ILE642
A	GLU643
A	CYS645
A	ALA646

---

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 1002

Chain	Residue
A	SER791
A	LEU792
A	ASP793
A	ARG806
A	HOH1161

---

site_id	AC3
Number of Residues	3
Details	binding site for residue SO4 A 1003

Chain	Residue
A	LYS777
A	LYS837
A	PRO959

---

site_id	AC4
Number of Residues	3
Details	binding site for residue SO4 A 1004

Chain	Residue
A	ARG594
A	ARG627
A	ARG919

---

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 A 1005

Chain	Residue
A	ARG722
A	HIS723
A	SER724
A	HOH1102

---

site_id	AC6
Number of Residues	3
Details	binding site for residue SO4 A 1006

Chain	Residue
A	GLY865
A	ARG867
A	HOH1175

---

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO A 1007

Chain	Residue
A	GLU664
A	HOH1119

---

site_id	AC8
Number of Residues	7
Details	binding site for residue EPE A 1008

Chain	Residue
A	HIS680
A	SER681
A	ASN683
A	TYR753
A	SER822
A	HOH1168
A	HOH1169

---

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	1
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP688

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU577

---

site_id	SWS_FT_FI3
Number of Residues	1
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

---

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

Chain	Residue	Details
A	GLU643
A	LYS690
A	ASP711

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Interacts with hydroxy-aryl-aldehyde inhibitors => ECO:0000250|UniProtKB:Q9EQY0

Chain	Residue	Details
A	TYR892

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:30118681

Chain	Residue	Details
A	SER724
A	SER729

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	THR973

---