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6KHE

Crystal structure of CLK2 in complex with CX-4945

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0006468biological_processprotein phosphorylation
A0010212biological_processresponse to ionizing radiation
A0016301molecular_functionkinase activity
A0016604cellular_componentnuclear body
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0042802molecular_functionidentical protein binding
A0043484biological_processregulation of RNA splicing
A0045721biological_processnegative regulation of gluconeogenesis
A0046777biological_processprotein autophosphorylation
A0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue 3NG A 1000
ChainResidue
ALEU169
ALEU245
ALEU246
ALEU297
AVAL326
AASP327
AHOH1115
AGLY170
AGLU171
APHE174
AVAL177
AALA191
ALYS193
APHE243
AGLU244

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGTFGRVVqCvdhrrggar.........VALK
ChainResidueDetails
ALEU169-LYS193

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LtHtDLKpeNILF
ChainResidueDetails
ALEU286-PHE298

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues316
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
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 Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by PKB/AKT2","evidences":[{"source":"UniProtKB","id":"O35491","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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