3R1M
Structure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006740 | biological_process | NADPH regeneration |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042132 | molecular_function | fructose 1,6-bisphosphate 1-phosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 13P A 401 |
| Chain | Residue |
| A | ASP12 |
| A | ASP234 |
| A | ARG266 |
| A | ASP287 |
| A | HOH386 |
| A | HOH388 |
| A | MG402 |
| A | MG403 |
| A | MG404 |
| A | HOH590 |
| A | HIS19 |
| A | ASP53 |
| A | GLN95 |
| A | ASP132 |
| A | LYS133 |
| A | TYR229 |
| A | GLY231 |
| A | LYS232 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | LYS232 |
| A | ASP234 |
| A | HOH386 |
| A | HOH388 |
| A | HOH389 |
| A | 13P401 |
| A | MG403 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ASP53 |
| A | ASP54 |
| A | ASP132 |
| A | ASP234 |
| A | HOH386 |
| A | 13P401 |
| A | MG402 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 404 |
| Chain | Residue |
| A | ASP12 |
| A | HIS19 |
| A | ASP53 |
| A | GLN95 |
| A | HOH387 |
| A | 13P401 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A 405 |
| Chain | Residue |
| A | HIS23 |
| A | PRO24 |
| A | HOH559 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor; for FBP phosphatase activity => ECO:0000305|PubMed:15274916, ECO:0000305|PubMed:21983966 |
| Chain | Residue | Details |
| A | ASP12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor; for FBP aldolase activity => ECO:0000305|PubMed:21983966 |
| Chain | Residue | Details |
| A | TYR229 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: Schiff-base intermediate with DHAP; for FBP aldolase activity => ECO:0000269|PubMed:21983966 |
| Chain | Residue | Details |
| A | LYS232 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:21983966, ECO:0007744|PDB:1UMG, ECO:0007744|PDB:3R1M |
| Chain | Residue | Details |
| A | ASP12 | |
| A | HIS19 | |
| A | ASP53 | |
| A | ASP54 | |
| A | GLN95 | |
| A | ASP132 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:15274916, ECO:0007744|PDB:1UMG |
| Chain | Residue | Details |
| A | TYR91 | |
| A | GLY104 | |
| A | TYR348 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21983966, ECO:0007744|PDB:3R1M |
| Chain | Residue | Details |
| A | LYS133 | |
| A | ARG266 | |
| A | ASP287 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21983966 |
| Chain | Residue | Details |
| A | LYS232 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15274916 |
| Chain | Residue | Details |
| A | ASP233 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15274916, ECO:0000269|PubMed:21983966 |
| Chain | Residue | Details |
| A | ASP234 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15274916, ECO:0007744|PDB:1UMG |
| Chain | Residue | Details |
| A | GLN242 |
