5TLW
Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor 1-phosphate-benzene 4-bisphosphonate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030335 | biological_process | positive regulation of cell migration |
| A | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| A | 0031430 | cellular_component | M band |
| A | 0031674 | cellular_component | I band |
| A | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030335 | biological_process | positive regulation of cell migration |
| B | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| B | 0031430 | cellular_component | M band |
| B | 0031674 | cellular_component | I band |
| B | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030335 | biological_process | positive regulation of cell migration |
| C | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| C | 0031430 | cellular_component | M band |
| C | 0031674 | cellular_component | I band |
| C | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030335 | biological_process | positive regulation of cell migration |
| D | 0030388 | biological_process | fructose 1,6-bisphosphate metabolic process |
| D | 0031430 | cellular_component | M band |
| D | 0031674 | cellular_component | I band |
| D | 0034316 | biological_process | negative regulation of Arp2/3 complex-mediated actin nucleation |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue RD3 A 401 |
| Chain | Residue |
| A | GLU34 |
| A | SER35 |
| A | SER38 |
| A | LYS107 |
| A | LYS146 |
| A | ARG148 |
| A | ARG303 |
| A | HOH515 |
| A | HOH578 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | LEU127 |
| A | GLU165 |
| A | ASN168 |
| A | ARG172 |
| A | HOH503 |
| A | HOH541 |
| B | LEU127 |
| B | GLU165 |
| B | ASN168 |
| B | HOH536 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue RD3 B 401 |
| Chain | Residue |
| B | ASP33 |
| B | GLU34 |
| B | SER35 |
| B | SER38 |
| B | LYS41 |
| B | LYS107 |
| B | LYS146 |
| B | ARG148 |
| B | ARG303 |
| B | HOH508 |
| B | HOH543 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue RD3 C 401 |
| Chain | Residue |
| C | SER35 |
| C | SER38 |
| C | LYS107 |
| C | LYS146 |
| C | ARG148 |
| C | ARG303 |
| C | HOH501 |
| C | HOH506 |
| C | HOH513 |
| C | HOH521 |
| C | HOH557 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue GOL C 402 |
| Chain | Residue |
| C | LEU127 |
| C | GLU165 |
| C | ASN168 |
| C | ARG172 |
| C | HOH556 |
| D | LEU127 |
| D | GLU165 |
| D | ASN168 |
| D | ARG172 |
| D | HOH519 |
| D | HOH563 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue RD3 D 401 |
| Chain | Residue |
| D | GLU34 |
| D | SER35 |
| D | SER38 |
| D | LYS107 |
| D | LYS146 |
| D | ARG148 |
| D | ARG303 |
| D | HOH511 |
| D | HOH514 |
| D | HOH535 |
| D | HOH587 |
Functional Information from PROSITE/UniProt
| site_id | PS00158 |
| Number of Residues | 11 |
| Details | ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN |
| Chain | Residue | Details |
| A | ILE221-ASN231 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11779856 |
| Chain | Residue | Details |
| A | GLU187 | |
| B | GLU187 | |
| C | GLU187 | |
| D | GLU187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Schiff-base intermediate with dihydroxyacetone-P => ECO:0000269|PubMed:11779856 |
| Chain | Residue | Details |
| A | LYS229 | |
| B | LYS229 | |
| C | LYS229 | |
| D | LYS229 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD |
| Chain | Residue | Details |
| A | ARG42 | |
| C | SER271 | |
| C | SER300 | |
| C | ARG303 | |
| D | ARG42 | |
| D | SER271 | |
| D | SER300 | |
| D | ARG303 | |
| A | SER271 | |
| A | SER300 | |
| A | ARG303 | |
| B | ARG42 | |
| B | SER271 | |
| B | SER300 | |
| B | ARG303 | |
| C | ARG42 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Essential for substrate cleavage |
| Chain | Residue | Details |
| A | CYS72 | |
| A | LYS107 | |
| B | CYS72 | |
| B | LYS107 | |
| C | CYS72 | |
| C | LYS107 | |
| D | CYS72 | |
| D | LYS107 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Alkylation inactivates the enzyme |
| Chain | Residue | Details |
| A | LYS146 | |
| B | LYS146 | |
| C | LYS146 | |
| D | LYS146 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base |
| Chain | Residue | Details |
| A | HIS361 | |
| B | HIS361 | |
| C | HIS361 | |
| D | HIS361 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | SITE: Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate |
| Chain | Residue | Details |
| A | TYR363 | |
| B | TYR363 | |
| C | TYR363 | |
| D | TYR363 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | THR8 | |
| B | THR8 | |
| C | THR8 | |
| D | THR8 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | SER35 | |
| C | SER38 | |
| C | SER45 | |
| C | SER271 | |
| D | SER35 | |
| D | SER38 | |
| D | SER45 | |
| D | SER271 | |
| A | SER38 | |
| A | SER45 | |
| A | SER271 | |
| B | SER35 | |
| B | SER38 | |
| B | SER45 | |
| B | SER271 | |
| C | SER35 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | LYS41 | |
| B | LYS41 | |
| C | LYS41 | |
| D | LYS41 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | LYS98 | |
| A | LYS146 | |
| B | LYS98 | |
| B | LYS146 | |
| C | LYS98 | |
| C | LYS146 | |
| D | LYS98 | |
| D | LYS146 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | LYS107 | |
| A | LYS329 | |
| B | LYS107 | |
| B | LYS329 | |
| C | LYS107 | |
| C | LYS329 | |
| D | LYS107 | |
| D | LYS329 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS110 | |
| B | LYS110 | |
| C | LYS110 | |
| D | LYS110 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05065 |
| Chain | Residue | Details |
| A | SER131 | |
| B | SER131 | |
| C | SER131 | |
| D | SER131 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS311 | |
| B | LYS311 | |
| C | LYS311 | |
| D | LYS311 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | MOD_RES: Deamidated asparagine; in form beta => ECO:0000269|PubMed:4857186 |
| Chain | Residue | Details |
| A | ASN360 | |
| B | ASN360 | |
| C | ASN360 | |
| D | ASN360 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | LYS41 | |
| B | LYS41 | |
| C | LYS41 | |
| D | LYS41 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| A | ASP33 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS146 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU187 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| A | GLU189 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| A | LYS229 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
| A | SER300 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | TYR363 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| B | ASP33 | electrostatic stabiliser, hydrogen bond acceptor |
| B | LYS146 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU187 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| B | GLU189 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| B | LYS229 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
| B | SER300 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | TYR363 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| C | ASP33 | electrostatic stabiliser, hydrogen bond acceptor |
| C | LYS146 | electrostatic stabiliser, hydrogen bond donor |
| C | GLU187 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| C | GLU189 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| C | LYS229 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
| C | SER300 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | TYR363 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 7 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| D | ASP33 | electrostatic stabiliser, hydrogen bond acceptor |
| D | LYS146 | electrostatic stabiliser, hydrogen bond donor |
| D | GLU187 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| D | GLU189 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| D | LYS229 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor, proton relay |
| D | SER300 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| D | TYR363 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
