4G31

Crystal Structure of GSK6414 Bound to PERK (R587-R1092, delete A660-T867) at 2.28 A Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 1101

Chain	Residue
A	HIS647
A	PRO648
A	GLY649
A	GLN919
A	GLU922
A	ALA923
A	VAL949
A	VAL950

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site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 0WH A 1102

Chain	Residue
A	VAL639
A	LEU642
A	ALA643
A	VAL651
A	TYR653
A	ILE885
A	MET887
A	GLN888
A	CYS890
A	PHE943
A	GLY953
A	ASP954
A	PHE955
A	HOH1355
A	HOH1356
A	ALA619

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGGFGVVFeAknkvddcn..........YAIK

Chain	Residue	Details
A	LEU598-LYS621

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

Chain	Residue	Details
A	LEU932-PHE944

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP936

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

Chain	Residue	Details
A	LEU598
A	LYS621

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:22169477

Chain	Residue	Details
A	TYR618

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231

Chain	Residue	Details
A	GLU922

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9Z2B5

Chain	Residue	Details
A	THR981

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