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1YXU

Crystal Structure of Kinase Pim1 in Complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0007346biological_processregulation of mitotic cell cycle
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0030145molecular_functionmanganese ion binding
A0043066biological_processnegative regulation of apoptotic process
A0045824biological_processnegative regulation of innate immune response
A0045893biological_processpositive regulation of DNA-templated transcription
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
B0000166molecular_functionnucleotide binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0007346biological_processregulation of mitotic cell cycle
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0030145molecular_functionmanganese ion binding
B0043066biological_processnegative regulation of apoptotic process
B0045824biological_processnegative regulation of innate immune response
B0045893biological_processpositive regulation of DNA-templated transcription
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
B0090336biological_processpositive regulation of brown fat cell differentiation
B0106310molecular_functionprotein serine kinase activity
B1902033biological_processregulation of hematopoietic stem cell proliferation
B1904263biological_processpositive regulation of TORC1 signaling
B1905062biological_processpositive regulation of cardioblast proliferation
C0000166molecular_functionnucleotide binding
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005730cellular_componentnucleolus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006468biological_processprotein phosphorylation
C0006915biological_processapoptotic process
C0007346biological_processregulation of mitotic cell cycle
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0030145molecular_functionmanganese ion binding
C0043066biological_processnegative regulation of apoptotic process
C0045824biological_processnegative regulation of innate immune response
C0045893biological_processpositive regulation of DNA-templated transcription
C0046872molecular_functionmetal ion binding
C0050821biological_processprotein stabilization
C0060045biological_processpositive regulation of cardiac muscle cell proliferation
C0070561biological_processvitamin D receptor signaling pathway
C0071346biological_processcellular response to type II interferon
C0090336biological_processpositive regulation of brown fat cell differentiation
C0106310molecular_functionprotein serine kinase activity
C1902033biological_processregulation of hematopoietic stem cell proliferation
C1904263biological_processpositive regulation of TORC1 signaling
C1905062biological_processpositive regulation of cardioblast proliferation
D0000166molecular_functionnucleotide binding
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006468biological_processprotein phosphorylation
D0006915biological_processapoptotic process
D0007346biological_processregulation of mitotic cell cycle
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0030145molecular_functionmanganese ion binding
D0043066biological_processnegative regulation of apoptotic process
D0045824biological_processnegative regulation of innate immune response
D0045893biological_processpositive regulation of DNA-templated transcription
D0046872molecular_functionmetal ion binding
D0050821biological_processprotein stabilization
D0060045biological_processpositive regulation of cardiac muscle cell proliferation
D0070561biological_processvitamin D receptor signaling pathway
D0071346biological_processcellular response to type II interferon
D0090336biological_processpositive regulation of brown fat cell differentiation
D0106310molecular_functionprotein serine kinase activity
D1902033biological_processregulation of hematopoietic stem cell proliferation
D1904263biological_processpositive regulation of TORC1 signaling
D1905062biological_processpositive regulation of cardioblast proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE IMD A 500
ChainResidue
APHE130
ATHR134
AASP170
AASP234
AGLY238
AASP239

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD B 600
ChainResidue
BASP170
BASP234
BGLY238
BASP239
BPHE130
BILE133
BTHR134

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IMD C 700
ChainResidue
CPHE130
CTHR134
CASP170
CASP234
CGLY238

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE IMD D 800
ChainResidue
DPHE130
DILE133
DTHR134
DASP170
DASP234
DGLY238
DASP239

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP A 550
ChainResidue
ALEU44
APHE49
AALA65
ALYS67
AGLU89
AILE104
ALEU120
AGLU171
AASN172
ALEU174
AILE185
AASP186
AHOH626

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AMP B 650
ChainResidue
BLEU44
BPHE49
BVAL52
BALA65
BLYS67
BILE104
BLEU120
BVAL126
BGLU171
BASN172
BILE185
BASP186

site_idAC7
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AMP C 750
ChainResidue
CLEU44
CPHE49
CALA65
CLYS67
CILE104
CLEU120
CARG122
CVAL126
CGLU171
CASN172
CLEU174
CILE185
CASP186

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AMP D 850
ChainResidue
DPHE49
DVAL52
DALA65
DLYS67
DGLU89
DILE104
DLEU120
DGLU121
DARG122
DLEU174
DILE185
DASP186

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 Residues1008
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15525646","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15657054","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15808862","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15657054","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR204
BLYS169
BASP167

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CTHR204
CLYS169
CASP167

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DTHR204
DLYS169
DASP167

site_idCSA13
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASN172
ALYS169
AASP167

site_idCSA14
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASN172
BLYS169
BASP167

site_idCSA15
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASN172
CLYS169
CASP167

site_idCSA16
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASN172
DLYS169
DASP167

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP167
BGLU171

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CASP167
CGLU171

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DASP167
DGLU171

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS169
AASP167

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS169
BASP167

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
CLYS169
CASP167

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
DLYS169
DASP167

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR204
ALYS169
AASP167

246704

PDB entries from 2025-12-24

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