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5UIS

Crystal structure of IRAK4 in complex with compound 12

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
B0000287molecular_functionmagnesium ion binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007165biological_processsignal transduction
C0000287molecular_functionmagnesium ion binding
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
C0007165biological_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 Residues11
Detailsbinding site for residue 8C1 A 800
ChainResidue
AGLU194
ALEU318
AHOH902
AVAL200
AALA211
AVAL263
ATYR264
AMET265
AGLY268
AALA315
AASN316

site_idAC2
Number of Residues10
Detailsbinding site for residue 8C1 B 801
ChainResidue
BGLU194
BALA211
BVAL263
BTYR264
BMET265
BGLY268
BALA315
BASN316
BLEU318
BHOH912

site_idAC3
Number of Residues11
Detailsbinding site for residue 8C1 C 501
ChainResidue
CGLU194
CALA211
CTYR262
CVAL263
CTYR264
CMET265
CGLY268
CALA315
CASN316
CLEU318
CHOH618

site_idAC4
Number of Residues10
Detailsbinding site for residue 8C1 D 501
ChainResidue
DMET192
DGLU194
DALA211
DVAL263
DTYR264
DMET265
DGLY268
DALA315
DLEU318
DHOH619

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2006","submissionDatabase":"PDB data bank","title":"Crystal structures of the apo and inhibited IRAK4 kinase domain.","authors":["Mol C.D.","Arduini R.M.","Baker D.P.","Chien E.Y.","Dougan D.R.","Friedman J.","Gibaja V.","Hession C.A.","Horne A."]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17161373","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2006","submissionDatabase":"PDB data bank","title":"Crystal structures of the apo and inhibited IRAK4 kinase domain.","authors":["Mol C.D.","Arduini R.M.","Baker D.P.","Chien E.Y.","Dougan D.R.","Friedman J.","Gibaja V.","Hession C.A.","Horne A."]}}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17161373","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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