5HGI

Crystal structure of apo human IRE1 alpha

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	3
Details	binding site for residue CS A 1000

Chain	Residue
A	ASP620
A	HIS622
A	VAL625

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CS A 1001

Chain	Residue
A	SER769
A	GLU770
A	GOL1006
A	GOL1006

---

site_id	AC3
Number of Residues	1
Details	binding site for residue CS A 1002

Chain	Residue
A	HIS680

---

site_id	AC4
Number of Residues	2
Details	binding site for residue CS A 1004

Chain	Residue
A	BME1011
A	BME1010

---

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

Chain	Residue
A	GLU949
A	LEU950
A	SER952
A	HIS953

---

site_id	AC6
Number of Residues	4
Details	binding site for residue GOL A 1006

Chain	Residue
A	GLU770
A	SER772
A	CS1001
A	CS1001

---

site_id	AC7
Number of Residues	4
Details	binding site for residue DTT A 1007

Chain	Residue
A	GLU807
A	HIS825
A	TYR945
A	GLU949

---

site_id	AC8
Number of Residues	1
Details	binding site for residue BME A 1008

Chain	Residue
A	ARG864

---

site_id	AC9
Number of Residues	2
Details	binding site for residue BME A 1009

Chain	Residue
A	ALA789
A	SER791

---

site_id	AD1
Number of Residues	3
Details	binding site for residue BME A 1010

Chain	Residue
A	ILE666
A	ILE768
A	CS1004

---

site_id	AD2
Number of Residues	1
Details	binding site for residue BME A 1011

Chain	Residue
A	CS1004

---

site_id	AD3
Number of Residues	1
Details	binding site for residue CL A 1013

Chain	Residue
A	LYS704

---

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

---