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6EGF

Crystal structure of the inactive unphosphorylated IRAK4 kinase domain bound to AMP-PNP

Functional Information from GO Data
ChainGOidnamespacecontents
B0000287molecular_functionmagnesium ion binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007165biological_processsignal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ANP B 501
ChainResidue
BMET192
BSER269
BASN311
BLYS313
BALA315
BASN316
BLEU318
BASP329
BMG504
BHOH631
BGLU194
BGLY195
BGLY196
BVAL200
BALA211
BLYS213
BVAL263
BMET265

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 B 502
ChainResidue
BHIS438
BGLU439
BLYS440

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 B 503
ChainResidue
BHIS307
BILE308
BARG334

site_idAC4
Number of Residues3
Detailsbinding site for residue MG B 504
ChainResidue
BASN316
BASP329
BANP501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BASN311

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BMET192

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING:
ChainResidueDetails
BLYS213
BLYS313
BASP329

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32
ChainResidueDetails
BTHR342

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:17161373, ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32
ChainResidueDetails
BTHR345

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17161373, ECO:0000269|PubMed:17312103
ChainResidueDetails
BSER346

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PDB entries from 2024-10-09

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