3CO7
Crystal Structure of FoxO1 DBD Bound to DBE2 DNA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0043565 | molecular_function | sequence-specific DNA binding |
| F | 0003700 | molecular_function | DNA-binding transcription factor activity |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PROSITE/UniProt
| site_id | PS00658 |
| Number of Residues | 7 |
| Details | FORK_HEAD_2 Fork head domain signature 2. WKNSIRH |
| Chain | Residue | Details |
| C | TRP209-HIS215 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 152 |
| Details | DNA_BIND: Fork-head => ECO:0000255|PROSITE-ProRule:PRU00089 |
| Chain | Residue | Details |
| C | ALA159-SER235 | |
| F | ALA159-SER235 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | SITE: DNA-binding => ECO:0000269|PubMed:18786403 |
| Chain | Residue | Details |
| C | ASN158 | |
| C | TYR165 | |
| C | ARG225 | |
| F | ASN158 | |
| F | TYR165 | |
| F | ARG225 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:18786403, ECO:0000269|PubMed:19221179, ECO:0000269|PubMed:21245099 |
| Chain | Residue | Details |
| C | SER212 | |
| F | SER212 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:18786403 |
| Chain | Residue | Details |
| C | SER218 | |
| C | SER234 | |
| C | SER235 | |
| F | SER218 | |
| F | SER234 | |
| F | SER235 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9R1E0 |
| Chain | Residue | Details |
| F | LYS245 | |
| F | LYS248 | |
| C | LYS245 | |
| C | LYS248 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:18356527 |
| Chain | Residue | Details |
| C | SER249 | |
| F | SER249 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Omega-N-methylarginine; by PRMT1 => ECO:0000250|UniProtKB:Q9R1E0 |
| Chain | Residue | Details |
| F | ARG251 | |
| F | ARG253 | |
| C | ARG251 | |
| C | ARG253 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PKB/AKT1 and SGK1 => ECO:0000269|PubMed:10358075, ECO:0000269|PubMed:10358076, ECO:0000269|PubMed:11237865, ECO:0000269|PubMed:11980723, ECO:0000269|PubMed:31063815 |
| Chain | Residue | Details |
| C | SER256 | |
| F | SER256 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:20543840 |
| Chain | Residue | Details |
| C | LYS262 | |
| C | LYS265 | |
| F | LYS262 | |
| F | LYS265 |
