1LE5
Crystal structure of a NF-kB heterodimer bound to an IFNb-kB
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003677 | molecular_function | DNA binding |
A | 0003700 | molecular_function | DNA-binding transcription factor activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0003677 | molecular_function | DNA binding |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0003677 | molecular_function | DNA binding |
E | 0003700 | molecular_function | DNA-binding transcription factor activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0003677 | molecular_function | DNA binding |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
Functional Information from PROSITE/UniProt
site_id | PS01204 |
Number of Residues | 7 |
Details | REL_1 NF-kappa-B/Rel/dorsal domain signature. FRYvCEG |
Chain | Residue | Details |
B | PHE55-GLY61 | |
A | PHE34-GLY40 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: S-nitrosocysteine; alternate => ECO:0000250|UniProtKB:P19838 |
Chain | Residue | Details |
B | CYS59 | |
F | CYS59 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000255 |
Chain | Residue | Details |
B | SER335 | |
F | SER335 | |
E | LYS122 | |
E | LYS123 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | LIPID: S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate => ECO:0000250|UniProtKB:P19838 |
Chain | Residue | Details |
B | CYS59 | |
F | CYS59 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P19838 |
Chain | Residue | Details |
B | LYS323 | |
A | LYS221 | |
F | LYS323 | |
E | LYS221 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q04206 |
Chain | Residue | Details |
A | THR254 | |
E | THR254 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q04206 |
Chain | Residue | Details |
A | SER276 | |
E | SER276 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q04206 |
Chain | Residue | Details |
A | SER281 | |
E | SER281 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3) => ECO:0000250 |
Chain | Residue | Details |
A | LYS37 | |
E | LYS37 |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate => ECO:0000250 |
Chain | Residue | Details |
A | LYS122 | |
A | LYS123 | |
E | LYS122 | |
E | LYS123 |