3COA
Crystal Structure of FoxO1 DBD Bound to IRE 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 PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA C 1 |
Chain | Residue |
C | LEU217 |
C | SER218 |
C | HIS220 |
C | PHE223 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA F 2 |
Chain | Residue |
D | HOH13 |
F | LEU217 |
F | SER218 |
F | HIS220 |
F | PHE223 |
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 |
C | LYS245 | |
C | LYS248 | |
F | LYS245 | |
F | 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 |
C | ARG251 | |
C | ARG253 | |
F | ARG251 | |
F | 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 |