10OJ
The crystal structure of apo phosphofructokinase from Escherichia coli
Functional Information from PROSITE/UniProt
| site_id | PS00433 |
| Number of Residues | 19 |
| Details | PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RatvlGHiQRGGspvpyDR |
| Chain | Residue | Details |
| A | ARG257-ARG275 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2953977","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2975709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2975709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2975709","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P00512","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 365 |
| Chain | Residue | Details |
| A | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG86 | electrostatic stabiliser |
| A | ASP117 | metal ligand |
| A | THR139 | electrostatic stabiliser |
| A | ASP141 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| A | ASP143 | hydrogen bond acceptor, increase acidity, increase basicity |
| A | ARG185 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 365 |
| Chain | Residue | Details |
| B | GLY25 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG86 | electrostatic stabiliser |
| B | ASP117 | metal ligand |
| B | THR139 | electrostatic stabiliser |
| B | ASP141 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| B | ASP143 | hydrogen bond acceptor, increase acidity, increase basicity |
| B | ARG185 | electrostatic stabiliser |
