Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4E3C

X-ray crystal structure of human IKK2 in an active conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0004672molecular_functionprotein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
E0004672molecular_functionprotein kinase activity
E0005524molecular_functionATP binding
E0006468biological_processprotein phosphorylation
F0004672molecular_functionprotein kinase activity
F0005524molecular_functionATP binding
F0006468biological_processprotein phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNIVL
ChainResidueDetails
AILE141-LEU153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP145
BASP145
CASP145
DASP145
EASP145
FASP145

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU21
ELYS44
FLEU21
FLYS44
ALYS44
BLEU21
BLYS44
CLEU21
CLYS44
DLEU21
DLYS44
ELEU21

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphoserine; by TBK1 and PKC/PRKCZ => ECO:0000269|PubMed:10022904, ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893
ChainResidueDetails
AGLU177
BGLU177
CGLU177
DGLU177
EGLU177
FGLU177

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:15184672
ChainResidueDetails
ACYS179
BCYS179
CCYS179
DCYS179
ECYS179
FCYS179

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: (Microbial infection) O-acetylthreonine; by Yersinia YopJ => ECO:0000269|PubMed:17116858
ChainResidueDetails
ATHR180
BTHR180
CTHR180
DTHR180
ETHR180
FTHR180

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphoserine; by TBK1, PKC/PRKCZ and PDPK1 => ECO:0000269|PubMed:10022904, ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:16207722
ChainResidueDetails
AGLU181
BGLU181
CGLU181
DGLU181
EGLU181
FGLU181

site_idSWS_FT_FI7
Number of Residues6
DetailsMOD_RES: Hydroxyproline => ECO:0000269|PubMed:17114296
ChainResidueDetails
APRO191
BPRO191
CPRO191
DPRO191
EPRO191
FPRO191

site_idSWS_FT_FI8
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16267042
ChainResidueDetails
ALYS163
FLYS163
BLYS163
CLYS163
DLYS163
ELYS163

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon