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1XR1

Crystal structure of hPim-1 kinase in complex with AMP-PNP at 2.1 A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine 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
A0008134molecular_functiontranscription factor binding
A0016310biological_processphosphorylation
A0022898biological_processregulation of transmembrane transporter activity
A0030145molecular_functionmanganese ion binding
A0043024molecular_functionribosomal small subunit binding
A0043066biological_processnegative regulation of apoptotic process
A0043433biological_processnegative regulation of DNA-binding transcription factor activity
A0044024molecular_functionhistone H2AS1 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
A0090336biological_processpositive regulation of brown fat cell differentiation
A0106310molecular_functionprotein serine kinase activity
A1902033biological_processregulation of hematopoietic stem cell proliferation
A1904263biological_processpositive regulation of TORC1 signaling
A1905062biological_processpositive regulation of cardioblast proliferation
A1990748biological_processcellular detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASN172
AASP186
AANP501

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 402
ChainResidue
AASP186
AANP501

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ANP A 501
ChainResidue
AGLU121
AARG122
ALEU174
AASP186
AMG401
AMG402
AGLY50
AVAL52
AALA65
ALYS67

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: Phosphothreonine => ECO:0000269|PubMed:15657054
ChainResidueDetails
ATHR23

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15657054
ChainResidueDetails
ASER98
ASER261

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP167
AGLU171

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS169
AASP167

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR204
ALYS169
AASP167

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN172
ALYS169
AASP167

226707

PDB entries from 2024-10-30

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