Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2BIL

The human protein kinase Pim1 in complex with its consensus peptide Pimtide

Functional Information from GO Data
ChainGOidnamespacecontents
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004676molecular_function3-phosphoinositide-dependent protein kinase activity
B0004677molecular_functionDNA-dependent protein kinase activity
B0004679molecular_functionAMP-activated protein kinase activity
B0004694molecular_functioneukaryotic translation initiation factor 2alpha kinase activity
B0004711molecular_functionribosomal protein S6 kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006338biological_processchromatin remodeling
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0007346biological_processregulation of mitotic cell cycle
B0008134molecular_functiontranscription factor binding
B0022898biological_processregulation of transmembrane transporter activity
B0030145molecular_functionmanganese ion binding
B0035175molecular_functionhistone H3S10 kinase activity
B0035402molecular_functionhistone H3T11 kinase activity
B0035403molecular_functionhistone H3T6 kinase activity
B0035979molecular_functionhistone H2AXS139 kinase activity
B0043024molecular_functionribosomal small subunit binding
B0043066biological_processnegative regulation of apoptotic process
B0043433biological_processnegative regulation of DNA-binding transcription factor activity
B0044022molecular_functionhistone H3S28 kinase activity
B0044023molecular_functionhistone H4S1 kinase activity
B0044024molecular_functionhistone H2AS1 kinase activity
B0044025molecular_functionhistone H2BS14 kinase activity
B0045824biological_processnegative regulation of innate immune response
B0045893biological_processpositive regulation of DNA-templated transcription
B0046777biological_processprotein autophosphorylation
B0046872molecular_functionmetal ion binding
B0050821biological_processprotein stabilization
B0060045biological_processpositive regulation of cardiac muscle cell proliferation
B0070561biological_processvitamin D receptor signaling pathway
B0071346biological_processcellular response to type II interferon
B0072354molecular_functionhistone H3T3 kinase activity
B0072371molecular_functionhistone H2AS121 kinase activity
B0072518molecular_functionRho-dependent protein serine/threonine kinase activity
B0090336biological_processpositive regulation of brown fat cell differentiation
B0106310molecular_functionprotein serine kinase activity
B0140823molecular_functionhistone H2BS36 kinase activity
B0140855molecular_functionhistone H3S57 kinase activity
B0140857molecular_functionhistone H3T45 kinase activity
B1902033biological_processregulation of hematopoietic stem cell proliferation
B1904263biological_processpositive regulation of TORC1 signaling
B1905062biological_processpositive regulation of cardioblast proliferation
B1990244molecular_functionhistone H2AT120 kinase activity
B1990748biological_processcellular detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BI1 B1307
ChainResidue
AARG6
BARG122
BGLU171
BLEU174
BILE185
BASP186
BLEU44
BPHE49
BVAL52
BALA65
BLYS67
BILE104
BLEU120
BGLU121

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK
ChainResidueDetails
BLEU44-LYS67

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI
ChainResidueDetails
BVAL163-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
BASP167

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU44

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862
ChainResidueDetails
BLYS67
BGLU121
BASP128

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER8

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:15657054
ChainResidueDetails
BTHR23

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054
ChainResidueDetails
BSER98
BSER261

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP167
BGLU171

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS169
BASP167

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR204
BLYS169
BASP167

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN172
BLYS169
BASP167

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon