6SHJ
Escherichia coli AGPase in complex with FBP. Symmetry applied C2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005978 | biological_process | glycogen biosynthetic process |
| A | 0008878 | molecular_function | glucose-1-phosphate adenylyltransferase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0010170 | cellular_component | glucose-1-phosphate adenylyltransferase complex |
| A | 0016208 | molecular_function | AMP binding |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005978 | biological_process | glycogen biosynthetic process |
| B | 0008878 | molecular_function | glucose-1-phosphate adenylyltransferase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0010170 | cellular_component | glucose-1-phosphate adenylyltransferase complex |
| B | 0016208 | molecular_function | AMP binding |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005978 | biological_process | glycogen biosynthetic process |
| C | 0008878 | molecular_function | glucose-1-phosphate adenylyltransferase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0010170 | cellular_component | glucose-1-phosphate adenylyltransferase complex |
| C | 0016208 | molecular_function | AMP binding |
| C | 0016779 | molecular_function | nucleotidyltransferase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005978 | biological_process | glycogen biosynthetic process |
| D | 0008878 | molecular_function | glucose-1-phosphate adenylyltransferase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0010170 | cellular_component | glucose-1-phosphate adenylyltransferase complex |
| D | 0016208 | molecular_function | AMP binding |
| D | 0016779 | molecular_function | nucleotidyltransferase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PROSITE/UniProt
| site_id | PS00808 |
| Number of Residues | 20 |
| Details | ADP_GLC_PYROPHOSPH_1 ADP-glucose pyrophosphorylase signature 1. AGGrGTrLkdLTnkrAkPAV |
| Chain | Residue | Details |
| D | ALA26-VAL45 |
| site_id | PS00809 |
| Number of Residues | 9 |
| Details | ADP_GLC_PYROPHOSPH_2 ADP-glucose pyrophosphorylase signature 2. WYrGTADAV |
| Chain | Residue | Details |
| D | TRP113-VAL121 |
| site_id | PS00810 |
| Number of Residues | 11 |
| Details | ADP_GLC_PYROPHOSPH_3 ADP-glucose pyrophosphorylase signature 3. ASMGIYVFdaD |
| Chain | Residue | Details |
| D | ALA211-ASP221 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27545622, ECO:0000305|PubMed:2162151 |
| Chain | Residue | Details |
| D | LYS39 | |
| A | LYS39 | |
| B | LYS39 | |
| C | LYS39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27545622 |
| Chain | Residue | Details |
| D | ARG40 | |
| A | HIS46 | |
| A | ARG52 | |
| A | ARG130 | |
| A | GLU370 | |
| A | ARG386 | |
| A | ARG419 | |
| A | GLN429 | |
| B | ARG40 | |
| B | HIS46 | |
| B | ARG52 | |
| D | HIS46 | |
| B | ARG130 | |
| B | GLU370 | |
| B | ARG386 | |
| B | ARG419 | |
| B | GLN429 | |
| C | ARG40 | |
| C | HIS46 | |
| C | ARG52 | |
| C | ARG130 | |
| C | GLU370 | |
| D | ARG52 | |
| C | ARG386 | |
| C | ARG419 | |
| C | GLN429 | |
| D | ARG130 | |
| D | GLU370 | |
| D | ARG386 | |
| D | ARG419 | |
| D | GLN429 | |
| A | ARG40 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:2844780 |
| Chain | Residue | Details |
| D | TYR114 | |
| A | TYR114 | |
| B | TYR114 | |
| C | TYR114 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:27545622 |
| Chain | Residue | Details |
| D | GLY179 | |
| D | SER212 | |
| A | GLY179 | |
| A | SER212 | |
| B | GLY179 | |
| B | SER212 | |
| C | GLY179 | |
| C | SER212 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:1648099, ECO:0000305|PubMed:27545622 |
| Chain | Residue | Details |
| D | GLU194 | |
| A | GLU194 | |
| B | GLU194 | |
| C | GLU194 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | SITE: Could play a key role in the communication between the regulatory and the substrate sites => ECO:0000305|PubMed:21741429 |
| Chain | Residue | Details |
| D | GLN74 | |
| D | TRP113 | |
| A | GLN74 | |
| A | TRP113 | |
| B | GLN74 | |
| B | TRP113 | |
| C | GLN74 | |
| C | TRP113 |
