1GVF
Structure of tagatose-1,6-bisphosphate aldolase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009025 | molecular_function | tagatose-bisphosphate aldolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 2001059 | biological_process | D-tagatose 6-phosphate catabolic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009025 | molecular_function | tagatose-bisphosphate aldolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 2001059 | biological_process | D-tagatose 6-phosphate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 288 |
| Chain | Residue |
| A | HIS83 |
| A | HIS180 |
| A | HIS208 |
| A | PGH287 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 289 |
| Chain | Residue |
| A | PGH287 |
| A | ALA179 |
| A | GLY181 |
| A | TYR183 |
| A | GLY209 |
| A | SER211 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 288 |
| Chain | Residue |
| B | HIS83 |
| B | HIS180 |
| B | HIS208 |
| B | PGH287 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 289 |
| Chain | Residue |
| B | ALA179 |
| B | GLY181 |
| B | TYR183 |
| B | GLY209 |
| B | SER211 |
| B | PGH287 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PGH A 287 |
| Chain | Residue |
| A | ASP82 |
| A | HIS83 |
| A | ALA179 |
| A | HIS180 |
| A | GLY181 |
| A | HIS208 |
| A | GLY209 |
| A | ALA210 |
| A | SER211 |
| A | ASN230 |
| A | VAL231 |
| A | ALA232 |
| A | THR233 |
| A | ZN288 |
| A | NA289 |
| A | HOH2347 |
| A | HOH2348 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A1289 |
| Chain | Residue |
| A | SER2 |
| A | SER70 |
| A | HOH2349 |
| A | HOH2350 |
| B | EDO1291 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A1290 |
| Chain | Residue |
| A | LEU9 |
| A | PRO44 |
| A | VAL45 |
| A | PRO76 |
| A | LEU77 |
| A | ALA78 |
| A | HOH2117 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A1291 |
| Chain | Residue |
| A | ASP190 |
| A | ARG193 |
| A | GLU196 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A1292 |
| Chain | Residue |
| A | GLN32 |
| A | GLU36 |
| A | TYR73 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A1293 |
| Chain | Residue |
| A | TYR63 |
| A | HIS95 |
| A | ALA96 |
| A | HOH2352 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A1294 |
| Chain | Residue |
| A | LEU9 |
| A | ASP12 |
| A | TYR18 |
| A | PRO44 |
| A | ARG283 |
| A | ILE284 |
| A | HOH2353 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PGH B 287 |
| Chain | Residue |
| B | ASN24 |
| B | ASP82 |
| B | HIS83 |
| B | ALA179 |
| B | HIS180 |
| B | GLY181 |
| B | HIS208 |
| B | GLY209 |
| B | ALA210 |
| B | SER211 |
| B | ASN230 |
| B | VAL231 |
| B | ALA232 |
| B | THR233 |
| B | ZN288 |
| B | NA289 |
| B | HOH2296 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1288 |
| Chain | Residue |
| B | PRO44 |
| B | VAL45 |
| B | PRO76 |
| B | LEU77 |
| B | ALA78 |
| B | HOH2298 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B1289 |
| Chain | Residue |
| B | SER2 |
| B | SER70 |
| B | MET75 |
| B | HOH2299 |
| B | HOH2300 |
| B | HOH2301 |
| B | HOH2302 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B1290 |
| Chain | Residue |
| B | HIS95 |
| B | ALA96 |
| B | HOH2303 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1291 |
| Chain | Residue |
| A | ASN74 |
| A | PRO76 |
| A | EDO1289 |
| B | HIS95 |
| B | GLN127 |
| B | EDO1292 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B1292 |
| Chain | Residue |
| A | ASN74 |
| B | HIS95 |
| B | GLU199 |
| B | EDO1291 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B1293 |
| Chain | Residue |
| B | SER106 |
| B | PHE108 |
| B | ARG137 |
| B | HOH2132 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B1294 |
| Chain | Residue |
| B | VAL114 |
| B | LYS115 |
| B | LYS118 |
| B | HOH2136 |
| B | HOH2140 |
| B | HOH2304 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B1295 |
| Chain | Residue |
| B | ARG91 |
| B | ASP122 |
| B | PHE123 |
| B | HOH2305 |
Functional Information from PROSITE/UniProt
| site_id | PS00602 |
| Number of Residues | 14 |
| Details | ALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. TtynMPLa.LHlDHH |
| Chain | Residue | Details |
| A | THR71-HIS84 |
| site_id | PS00806 |
| Number of Residues | 12 |
| Details | ALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. VEaELGrlGGvE |
| Chain | Residue | Details |
| A | VAL131-GLU142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11940603","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11940603","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b57 |
| Chain | Residue | Details |
| A | ASP82 | |
| A | ASN230 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b57 |
| Chain | Residue | Details |
| B | ASP82 | |
| B | GLU150 | |
| B | ASN230 |
