eF-site ID 3coa-F PDB Code 3coa Chain F click to enlarge Title Crystal Structure of FoxO1 DBD Bound to IRE DNA Classification Transcription/DNA Compound DNA (5'-D(*DTP*DGP*DGP*DTP*DTP*DTP*DGP*DTP*DTP*DTP*DTP*DGP*DCP*DTP*DTP*DG)-3') Source Homo sapiens (Human) (3COA) Sequence F:  SRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSV PYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKS SWWMLNP Description Functional site 1) chain F residue 217 type sequence L description BINDING SITE FOR RESIDUE CA F 2 source : AC2 2) chain F residue 218 type sequence S description BINDING SITE FOR RESIDUE CA F 2 source : AC2 3) chain F residue 220 type sequence H description BINDING SITE FOR RESIDUE CA F 2 source : AC2 4) chain F residue 223 type sequence F description BINDING SITE FOR RESIDUE CA F 2 source : AC2 5) chain F residue 159-235 type DNA_BIND sequence AWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFK DKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSS description Fork-head => ECO:0000255|PROSITE-ProRule:PRU00089 source Swiss-Prot : SWS_FT_FI1 6) chain F residue 212 type MOD_RES sequence S description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:18786403, ECO:0000269|PubMed:19221179, ECO:0000269|PubMed:21245099 source Swiss-Prot : SWS_FT_FI3 7) chain F residue 218 type MOD_RES sequence S description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:18786403 source Swiss-Prot : SWS_FT_FI4 8) chain F residue 234 type MOD_RES sequence S description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:18786403 source Swiss-Prot : SWS_FT_FI4 9) chain F residue 235 type MOD_RES sequence S description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:18786403 source Swiss-Prot : SWS_FT_FI4 10) chain F residue 158 type SITE sequence N description DNA-binding => ECO:0000269|PubMed:18786403 source Swiss-Prot : SWS_FT_FI2 11) chain F residue 165 type SITE sequence Y description DNA-binding => ECO:0000269|PubMed:18786403 source Swiss-Prot : SWS_FT_FI2 12) chain F residue 225 type SITE sequence R description DNA-binding => ECO:0000269|PubMed:18786403 source Swiss-Prot : SWS_FT_FI2

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