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5NDT

Crystal structure of human Pim-1 kinase in complex with a consensus peptide and fragment like molecule (E)-3-(2-(thiophen-2-yl)vinyl)-3,4-dihydroquinoxalin-2(1H)-one

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004676molecular_function3-phosphoinositide-dependent protein kinase activity
A0004677molecular_functionDNA-dependent protein kinase activity
A0004679molecular_functionAMP-activated protein kinase activity
A0004694molecular_functioneukaryotic translation initiation factor 2alpha kinase activity
A0004711molecular_functionribosomal protein S6 kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006338biological_processchromatin remodeling
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007346biological_processregulation of mitotic cell cycle
A0008134molecular_functiontranscription factor binding
A0022898biological_processregulation of transmembrane transporter activity
A0030145molecular_functionmanganese ion binding
A0035175molecular_functionhistone H3S10 kinase activity
A0035402molecular_functionhistone H3T11 kinase activity
A0035403molecular_functionhistone H3T6 kinase activity
A0035979molecular_functionhistone H2AXS139 kinase activity
A0043024molecular_functionribosomal small subunit binding
A0043066biological_processnegative regulation of apoptotic process
A0043433biological_processnegative regulation of DNA-binding transcription factor activity
A0044022molecular_functionhistone H3S28 kinase activity
A0044023molecular_functionhistone H4S1 kinase activity
A0044024molecular_functionhistone H2AS1 kinase activity
A0044025molecular_functionhistone H2BS14 kinase activity
A0045824biological_processnegative regulation of innate immune response
A0045893biological_processpositive regulation of DNA-templated transcription
A0046777biological_processprotein autophosphorylation
A0046872molecular_functionmetal ion binding
A0050821biological_processprotein stabilization
A0060045biological_processpositive regulation of cardiac muscle cell proliferation
A0070561biological_processvitamin D receptor signaling pathway
A0071346biological_processcellular response to type II interferon
A0072354molecular_functionhistone H3T3 kinase activity
A0072371molecular_functionhistone H2AS121 kinase activity
A0072518molecular_functionRho-dependent protein serine/threonine kinase activity
A0090336biological_processpositive regulation of brown fat cell differentiation
A0106310molecular_functionprotein serine kinase activity
A0140823molecular_functionhistone H2BS36 kinase activity
A0140855molecular_functionhistone H3S57 kinase activity
A0140857molecular_functionhistone H3T45 kinase activity
A1902033biological_processregulation of hematopoietic stem cell proliferation
A1904263biological_processpositive regulation of TORC1 signaling
A1905062biological_processpositive regulation of cardioblast proliferation
A1990244molecular_functionhistone H2AT120 kinase activity
A1990748biological_processcellular detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 401
ChainResidue
ATYR233
APRO241
AGLU247
AGLN252
APHE254
AARG256

site_idAC2
Number of Residues8
Detailsbinding site for residue 8UB A 402
ChainResidue
ALYS67
AGLU121
ALEU174
AHOH528
AHOH587
APHE49
AVAL52
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 Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER8

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:15657054
ChainResidueDetails
ATHR23

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054
ChainResidueDetails
ASER98
ASER261

227344

PDB entries from 2024-11-13

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