7B7Z
DeAMPylation complex of monomeric FICD and AMPylated BiP (state 1)
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00297 |
Number of Residues | 8 |
Details | HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS |
Chain | Residue | Details |
B | ILE33-SER40 |
site_id | PS00329 |
Number of Residues | 14 |
Details | HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGAfdvSLL |
Chain | Residue | Details |
B | VAL222-LEU235 |
site_id | PS01036 |
Number of Residues | 15 |
Details | HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ |
Chain | Residue | Details |
B | ILE359-GLN373 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:22266942 |
Chain | Residue | Details |
A | ALA363 | |
B | GLY227 | |
B | GLU293 | |
B | GLY364 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0U |
Chain | Residue | Details |
A | GLU234 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07, ECO:0007744|PDB:4U0S, ECO:0007744|PDB:4U0U |
Chain | Residue | Details |
A | TYR399 | |
A | ASN407 | |
A | VAL316 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25435325, ECO:0007744|PDB:4U07 |
Chain | Residue | Details |
B | LYS326 | |
A | ASP367 | |
B | LYS213 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for autoinhibition of adenylyltransferase activity => ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:25435325 |
Chain | Residue | Details |
A | GLU234 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: O-AMP-threonine; by autocatalysis => ECO:0000305|PubMed:25601083 |
Chain | Residue | Details |
A | THR183 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498, ECO:0000269|PubMed:25601083 |
Chain | Residue | Details |
A | ASN275 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P20029 |
Chain | Residue | Details |
B | LYS447 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P0DMV8 |
Chain | Residue | Details |
B | ARG492 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; alternate => ECO:0000250|UniProtKB:P11021 |
Chain | Residue | Details |
B | THR518 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P11021 |
Chain | Residue | Details |
B | LYS352 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P11021 |
Chain | Residue | Details |
B | LYS353 |