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6T29

Crystal structure of human calmodulin-dependent protein kinase 1D (CAMK1D) bound to compound 18 (CS587)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0004672molecular_functionprotein kinase activity
AAA0004674molecular_functionprotein serine/threonine kinase activity
AAA0004683molecular_functioncalmodulin-dependent protein kinase activity
AAA0005515molecular_functionprotein binding
AAA0005516molecular_functioncalmodulin binding
AAA0005524molecular_functionATP binding
AAA0005634cellular_componentnucleus
AAA0005737cellular_componentcytoplasm
AAA0006468biological_processprotein phosphorylation
AAA0006954biological_processinflammatory response
AAA0007399biological_processnervous system development
AAA0010976biological_processpositive regulation of neuron projection development
AAA0032793biological_processpositive regulation of CREB transcription factor activity
AAA0043065biological_processpositive regulation of apoptotic process
AAA0043066biological_processnegative regulation of apoptotic process
AAA0050766biological_processpositive regulation of phagocytosis
AAA0050773biological_processregulation of dendrite development
AAA0060267biological_processpositive regulation of respiratory burst
AAA0071622biological_processregulation of granulocyte chemotaxis
AAA0090023biological_processpositive regulation of neutrophil chemotaxis
AAA0106310molecular_functionprotein serine kinase activity
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGAFSEVVlAeekatgklfavkc.....IPKK
ChainResidueDetails
AAALEU29-LYS57

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLY
ChainResidueDetails
AAAILE140-TYR152

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
AAAASP144

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AAALEU29
AAALYS52

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
AAASER122

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMKK1 and CaMKK2 => ECO:0000269|PubMed:12935886, ECO:0007744|PubMed:18669648
ChainResidueDetails
AAATHR180

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
AAALYS113

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PDB entries from 2024-07-24

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