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6EGD

Crystal structure of the unphosphorylated IRAK4 kinase domain Bound to a type I inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
D0000287molecular_functionmagnesium ion binding
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
D0007165biological_processsignal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue J87 D 501
ChainResidue
DMET192
DLEU318
DSER328
DHOH609
DALA211
DLYS213
DTYR262
DVAL263
DTYR264
DMET265
DGLY268
DASP272

site_idAC2
Number of Residues13
Detailsbinding site for residue J87 A 501
ChainResidue
AMET192
AALA211
ALYS213
ATYR262
AVAL263
ATYR264
AMET265
APRO266
AGLY268
ALEU318
ASER328
AASP329
AHOH616

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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