4E3C
X-ray crystal structure of human IKK2 in an active conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
E | 0004672 | molecular_function | protein kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0004672 | molecular_function | protein kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNIVL |
Chain | Residue | Details |
A | ILE141-LEU153 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
A | ASP145 | |
B | ASP145 | |
C | ASP145 | |
D | ASP145 | |
E | ASP145 | |
F | ASP145 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
A | LEU21 | |
E | LYS44 | |
F | LEU21 | |
F | LYS44 | |
A | LYS44 | |
B | LEU21 | |
B | LYS44 | |
C | LEU21 | |
C | LYS44 | |
D | LEU21 | |
D | LYS44 | |
E | LEU21 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine; by TBK1 and PKC/PRKCZ => ECO:0000269|PubMed:10022904, ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893 |
Chain | Residue | Details |
A | GLU177 | |
B | GLU177 | |
C | GLU177 | |
D | GLU177 | |
E | GLU177 | |
F | GLU177 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:15184672 |
Chain | Residue | Details |
A | CYS179 | |
B | CYS179 | |
C | CYS179 | |
D | CYS179 | |
E | CYS179 | |
F | CYS179 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | MOD_RES: (Microbial infection) O-acetylthreonine; by Yersinia YopJ => ECO:0000269|PubMed:17116858 |
Chain | Residue | Details |
A | THR180 | |
B | THR180 | |
C | THR180 | |
D | THR180 | |
E | THR180 | |
F | THR180 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine; by TBK1, PKC/PRKCZ and PDPK1 => ECO:0000269|PubMed:10022904, ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:16207722 |
Chain | Residue | Details |
A | GLU181 | |
B | GLU181 | |
C | GLU181 | |
D | GLU181 | |
E | GLU181 | |
F | GLU181 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | MOD_RES: Hydroxyproline => ECO:0000269|PubMed:17114296 |
Chain | Residue | Details |
A | PRO191 | |
B | PRO191 | |
C | PRO191 | |
D | PRO191 | |
E | PRO191 | |
F | PRO191 |
site_id | SWS_FT_FI8 |
Number of Residues | 12 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16267042 |
Chain | Residue | Details |
A | LYS163 | |
F | LYS163 | |
B | LYS163 | |
C | LYS163 | |
D | LYS163 | |
E | LYS163 |