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8BFS

Crystal structure of human calmodulin-dependent protein kinase 1D (CAMK1D) in complex with FZ326

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004683molecular_functioncalcium/calmodulin-dependent protein kinase activity
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006468biological_processprotein phosphorylation
A0006954biological_processinflammatory response
A0007165biological_processsignal transduction
A0007399biological_processnervous system development
A0010975biological_processregulation of neuron projection development
A0010976biological_processpositive regulation of neuron projection development
A0032793biological_processpositive regulation of CREB transcription factor activity
A0043065biological_processpositive regulation of apoptotic process
A0043066biological_processnegative regulation of apoptotic process
A0050766biological_processpositive regulation of phagocytosis
A0050773biological_processregulation of dendrite development
A0060267biological_processpositive regulation of respiratory burst
A0071622biological_processregulation of granulocyte chemotaxis
A0090023biological_processpositive regulation of neutrophil chemotaxis
A0106310molecular_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
ALEU29-LYS57

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLY
ChainResidueDetails
AILE140-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
AASP144

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU29
ALYS52

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER122

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMKK1 and CaMKK2 => ECO:0000269|PubMed:12935886, ECO:0007744|PubMed:18669648
ChainResidueDetails
ATHR180

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
ALYS113

227344

PDB entries from 2024-11-13

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