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2BZI

CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH A RUTHENIUM ORGANOMETALLIC LIGAND RU2

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 Residues18
DetailsBINDING SITE FOR RESIDUE DW2 B1306
ChainResidue
BLEU44
BGLU121
BARG122
BASP128
BGLU171
BLEU174
BILE185
BASP186
BHOH2049
BHOH2268
BGLY45
BPHE49
BVAL52
BALA65
BLYS67
BGLU89
BILE104
BLEU120

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
BSEP261

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

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PDB entries from 2024-11-06

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