4X7K

Co-crystal Structure of PERK bound to 4-{2-amino-3-[5-fluoro-2-(methylamino)quinazolin-6-yl]-4-methylbenzoyl}-1-methyl-2,5-diphenyl-1,2-dihydro-3H-pyrazol-3-one inhibitor

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	15
Details	binding site for residue 3Z3 A 1101

Chain	Residue
A	VAL607
A	CYS891
A	ARG892
A	GLY954
A	ASP955
A	PHE956
A	GOL1103
A	ALA620
A	LYS622
A	GLU639
A	LEU643
A	VAL652
A	ILE886
A	MET888
A	GLN889

---

site_id	AC2
Number of Residues	12
Details	binding site for residue TLA A 1102

Chain	Residue
A	ARG629
A	LEU631
A	ALA632
A	TRP899
A	ARG903
A	HOH1205
A	HOH1212
A	HOH1229
A	HOH1230
A	HOH1232
A	HOH1234
A	HOH1245

---

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 1103

Chain	Residue
A	GLU639
A	ALA642
A	LEU933
A	MET934
A	HIS935
A	3Z31101
A	HOH1329

---

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	LEU599-LYS622

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"22169477","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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