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4X7H

Co-crystal Structure of PERK bound to N-{5-[(6,7-dimethoxyquinolin-4-yl)oxy]pyridin-2-yl}-1-methyl-3-oxo-2-phenyl-5-(pyridin-4-yl)-2,3-dihydro-1H-pyrazole-4-carboxamide inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue 3Z2 A 1101
ChainResidue
ALEU599
AHIS935
APHE944
AGLY954
AASP955
APHE956
AHOH1383
AALA620
ALYS622
AGLU639
AILE886
AMET888
AGLN889
ACYS891
ALYS893

site_idAC2
Number of Residues9
Detailsbinding site for residue SO4 A 1102
ChainResidue
AARG629
ALEU631
ALYS635
AGLU894
ATRP899
AARG903
AHOH1230
AHOH1236
AHOH1293

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 1103
ChainResidue
AARG601
APHE608
AARG623

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGGFGVVFeAknkvddcn..........YAIK
ChainResidueDetails
ALEU599-LYS622

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"22169477","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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