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5KX7

Irak4-inhibitor co-structure

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
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 6YD B 9901
ChainResidue
BMET192
BALA211
BLYS213
BVAL246
BTYR262
BVAL263
BMET265
BGLY268
BLEU318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP311
BASP311

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AMET192
BMET192

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ALYS213
ALYS313
AASP329
BLYS213
BLYS313
BASP329

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32
ChainResidueDetails
ATPO342
BTPO342

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:17161373, ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32
ChainResidueDetails
ATPO345
BTPO345

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17161373, ECO:0000269|PubMed:17312103
ChainResidueDetails
ASEP346
BSEP346

222624

PDB entries from 2024-07-17

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