6SHQ
Escherichia coli AGPase in complex with AMP. Symmetry C2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005978 | biological_process | glycogen biosynthetic process |
| A | 0008878 | molecular_function | glucose-1-phosphate adenylyltransferase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009250 | biological_process | glucan 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 | 0005978 | biological_process | glycogen biosynthetic process |
| B | 0008878 | molecular_function | glucose-1-phosphate adenylyltransferase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009250 | biological_process | glucan 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 | 0005978 | biological_process | glycogen biosynthetic process |
| C | 0008878 | molecular_function | glucose-1-phosphate adenylyltransferase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0009250 | biological_process | glucan 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 | 0005978 | biological_process | glycogen biosynthetic process |
| D | 0008878 | molecular_function | glucose-1-phosphate adenylyltransferase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0009250 | biological_process | glucan 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 PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue AMP A 501 |
| Chain | Residue |
| A | LYS39 |
| C | ARG130 |
| A | ARG40 |
| A | HIS46 |
| A | ARG52 |
| A | THR79 |
| A | GLU370 |
| A | ARG386 |
| A | ALA387 |
| A | ARG419 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue AMP D 501 |
| Chain | Residue |
| B | ARG130 |
| D | ARG40 |
| D | HIS46 |
| D | ARG52 |
| D | THR79 |
| D | GLU370 |
| D | ARG386 |
| D | ALA387 |
| D | ARG419 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue AMP C 501 |
| Chain | Residue |
| A | ARG130 |
| C | LYS39 |
| C | ARG40 |
| C | HIS46 |
| C | ARG52 |
| C | THR79 |
| C | GLU370 |
| C | ARG386 |
| C | ALA387 |
| C | ARG419 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue AMP B 501 |
| Chain | Residue |
| B | ARG40 |
| B | HIS46 |
| B | ARG52 |
| B | THR79 |
| B | GLU370 |
| B | ARG386 |
| B | ALA387 |
| B | ARG419 |
| D | ARG130 |
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 |
| A | ALA26-VAL45 |
| site_id | PS00809 |
| Number of Residues | 9 |
| Details | ADP_GLC_PYROPHOSPH_2 ADP-glucose pyrophosphorylase signature 2. WYrGTADAV |
| Chain | Residue | Details |
| A | TRP113-VAL121 |
| site_id | PS00810 |
| Number of Residues | 11 |
| Details | ADP_GLC_PYROPHOSPH_3 ADP-glucose pyrophosphorylase signature 3. ASMGIYVFdaD |
| Chain | Residue | Details |
| A | ALA211-ASP221 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27545622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2162151","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27545622","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"2844780","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27545622","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1648099","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27545622","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Site: {"description":"Could play a key role in the communication between the regulatory and the substrate sites","evidences":[{"source":"PubMed","id":"21741429","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
