8XI3
Structure of mouse SCMC-14-3-3gama complex
Functional Information from PROSITE/UniProt
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. ALAGftDgTVRIWDL |
Chain | Residue | Details |
B | ALA402-LEU416 |
site_id | PS00796 |
Number of Residues | 11 |
Details | 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV |
Chain | Residue | Details |
F | ARG42-VAL52 |
site_id | PS00797 |
Number of Residues | 20 |
Details | 1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS |
Chain | Residue | Details |
F | TYR216-SER235 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0000255 |
Chain | Residue | Details |
B | SEP139 | |
B | SER187 | |
B | SEP209 | |
D | ARG132 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9H808 |
Chain | Residue | Details |
B | SER519 | |
D | MET1 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylvaline; in 14-3-3 protein gamma, N-terminally processed => ECO:0000250|UniProtKB:P61981 |
Chain | Residue | Details |
F | VAL2 | |
D | VAL2 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
F | SER71 | |
D | SER71 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P61983 |
Chain | Residue | Details |
F | TYR133 | |
D | TYR133 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P61981 |
Chain | Residue | Details |
F | THR145 | |
F | THR234 | |
D | THR145 | |
D | THR234 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P61983 |
Chain | Residue | Details |
F | SER215 | |
D | SER215 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P61981 |
Chain | Residue | Details |
F | SER235 | |
D | SER235 |