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5IIS

Design, synthesis and structure activity relationship of potent pan-PIM kinase inhibitors derived from the pyridyl-amide scaffold

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0043066biological_processnegative regulation of apoptotic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue PEG A 401
ChainResidue
APHE130
AILE133
AASP170
ATYR207
AASP234
AASP239

site_idAC2
Number of Residues14
Detailsbinding site for residue 6CB A 402
ChainResidue
ALYS67
AILE104
ALEU120
AGLU121
AVAL126
AASP128
AGLU171
ALEU174
AILE185
AASP186
AHOH565
ALEU44
APHE49
AALA65

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK
ChainResidueDetails
ALEU44-LYS67

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI
ChainResidueDetails
AVAL163-ILE175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP167

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU44

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862
ChainResidueDetails
ALYS67
AGLU121
AASP128

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054
ChainResidueDetails
ASER98
ASEP261

225681

PDB entries from 2024-10-02

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