4Z7G

Crystal structure of human IRE1 cytoplasmic kinase-RNase region - apo

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

Functional Information from PDB Data

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

Chain	Residue
A	ASP620
A	HIS622
A	VAL625

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site_id	AC2
Number of Residues	3
Details	binding site for residue NA B 1001

Chain	Residue
B	ASP620
B	HIS622
B	VAL625

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
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

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU577
B	LEU577

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site_id	SWS_FT_FI3
Number of Residues	2
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

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site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:21317875, ECO:0007744|PDB:3P23

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

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site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Interacts with hydroxy-aryl-aldehyde inhibitors => ECO:0000250|UniProtKB:Q9EQY0

Chain	Residue	Details
A	TYR892
B	TYR892

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site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:30118681

Chain	Residue	Details
B	SER724
B	SER729
A	SER724
A	SER729

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	THR973
B	THR973

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