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2BUJ

Crystal structure of the human Serine-threonine Kinase 16 in complex with staurosporine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005798cellular_componentGolgi-associated vesicle
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006468biological_processprotein phosphorylation
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016604cellular_componentnuclear body
A0016740molecular_functiontransferase activity
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046777biological_processprotein autophosphorylation
A0048471cellular_componentperinuclear region of cytoplasm
A0071560biological_processcellular response to transforming growth factor beta stimulus
A0106310molecular_functionprotein serine kinase activity
B0000166molecular_functionnucleotide binding
B0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005798cellular_componentGolgi-associated vesicle
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006468biological_processprotein phosphorylation
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016604cellular_componentnuclear body
B0016740molecular_functiontransferase activity
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046777biological_processprotein autophosphorylation
B0048471cellular_componentperinuclear region of cytoplasm
B0071560biological_processcellular response to transforming growth factor beta stimulus
B0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A1300
ChainResidue
AARG59
ASTU1302

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B1298
ChainResidue
BGLY30
BSER32

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE STU A1301
ChainResidue
APHE100
APHE101
AMET165
ALEU26
AGLU28
AVAL34
AALA47
APRO99

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE STU A1302
ChainResidue
AGLU87
AHIS92
ACL1300
BGLN24
BSTU1300

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE STU B1299
ChainResidue
BLEU26
BGLY27
BGLU28
BALA47
BPRO99
BPHE100
BPHE101
BMET165
BSTU1300

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE STU B1300
ChainResidue
AHIS54
AGLU55
ASTU1302
BGLN24
BLEU26
BPHE45
BPHE100
BLYS102
BARG103
BGLY104
BSTU1299

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKptNILL
ChainResidueDetails
ATYR144-LEU156

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsRegion: {"description":"Activation loop"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
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 Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"18184589","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18184589","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"18184589","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR152
AASP148

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR152
BASP148

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP148
ALYS150

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP148
BLYS150

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR195
AASP148
ALYS150

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR195
BASP148
BLYS150

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP148
ALYS150
AASN153

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP148
BLYS150
BASN153

238895

PDB entries from 2025-07-16

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