1ADO
FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE
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 | 0006096 | biological_process | glycolytic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030335 | biological_process | positive regulation of cell migration |
| 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 | 0006096 | biological_process | glycolytic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030335 | biological_process | positive regulation of cell migration |
| 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 | 0006096 | biological_process | glycolytic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030335 | biological_process | positive regulation of cell migration |
| 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 | 0006096 | biological_process | glycolytic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030335 | biological_process | positive regulation of cell migration |
| 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 | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1326 |
| Chain | Residue |
| B | LYS12 |
| C | LYS199 |
| C | GLN202 |
| C | ARG258 |
| C | HOH1329 |
| C | HOH2014 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1261 |
| Chain | Residue |
| D | ARG258 |
| D | HOH1281 |
| D | HOH1376 |
| A | LYS12 |
| D | LYS199 |
| D | GLN202 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 13P A 1104 |
| Chain | Residue |
| A | ALA31 |
| A | ASP33 |
| A | ARG42 |
| A | LYS146 |
| A | ARG148 |
| A | GLU187 |
| A | LYS229 |
| A | LEU270 |
| A | SER271 |
| A | GLY272 |
| A | GLY273 |
| A | SER300 |
| A | TYR301 |
| A | GLY302 |
| A | ARG303 |
| A | HOH1333 |
| A | HOH1544 |
| A | HOH1579 |
| A | HOH1664 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 13P B 1053 |
| Chain | Residue |
| B | LEU270 |
| B | SER271 |
| B | GLY272 |
| B | GLY273 |
| B | SER300 |
| B | TYR301 |
| B | GLY302 |
| B | ARG303 |
| B | HOH1155 |
| B | HOH1238 |
| B | HOH1441 |
| B | HOH1563 |
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 | PRO188 | |
| B | PRO188 | |
| C | PRO188 | |
| D | PRO188 |
| 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 | PRO230 | |
| B | PRO230 | |
| C | PRO230 | |
| D | PRO230 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10504235, ECO:0007744|PDB:6ALD |
| Chain | Residue | Details |
| A | LEU43 | |
| C | GLY272 | |
| C | TYR301 | |
| C | ALA304 | |
| D | LEU43 | |
| D | GLY272 | |
| D | TYR301 | |
| D | ALA304 | |
| A | GLY272 | |
| A | TYR301 | |
| A | ALA304 | |
| B | LEU43 | |
| B | GLY272 | |
| B | TYR301 | |
| B | ALA304 | |
| C | LEU43 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Essential for substrate cleavage |
| Chain | Residue | Details |
| A | ILE73 | |
| A | VAL108 | |
| B | ILE73 | |
| B | VAL108 | |
| C | ILE73 | |
| C | VAL108 | |
| D | ILE73 | |
| D | VAL108 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Alkylation inactivates the enzyme |
| Chain | Residue | Details |
| A | TRP147 | |
| B | TRP147 | |
| C | TRP147 | |
| D | TRP147 |
| 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 | ALA362 | |
| B | ALA362 | |
| C | ALA362 | |
| D | ALA362 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | PRO9 | |
| B | PRO9 | |
| C | PRO9 | |
| D | PRO9 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 16 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | THR36 | |
| C | ILE39 | |
| C | ILE46 | |
| C | GLY272 | |
| D | THR36 | |
| D | ILE39 | |
| D | ILE46 | |
| D | GLY272 | |
| A | ILE39 | |
| A | ILE46 | |
| A | GLY272 | |
| B | THR36 | |
| B | ILE39 | |
| B | ILE46 | |
| B | GLY272 | |
| C | THR36 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | ARG42 | |
| B | ARG42 | |
| C | ARG42 | |
| D | ARG42 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | SER99 | |
| A | TRP147 | |
| B | SER99 | |
| B | TRP147 | |
| C | SER99 | |
| C | TRP147 | |
| D | SER99 | |
| D | TRP147 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P04075 |
| Chain | Residue | Details |
| A | VAL108 | |
| A | ARG330 | |
| B | VAL108 | |
| B | ARG330 | |
| C | VAL108 | |
| C | ARG330 | |
| D | VAL108 | |
| D | ARG330 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-malonyllysine; alternate => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY111 | |
| B | GLY111 | |
| C | GLY111 | |
| D | GLY111 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05065 |
| Chain | Residue | Details |
| A | GLU132 | |
| B | GLU132 | |
| C | GLU132 | |
| D | GLU132 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
| Chain | Residue | Details |
| A | ALA312 | |
| B | ALA312 | |
| C | ALA312 | |
| D | ALA312 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | MOD_RES: Deamidated asparagine; in form beta => ECO:0000269|PubMed:4857186 |
| Chain | Residue | Details |
| A | HIS361 | |
| B | HIS361 | |
| C | HIS361 | |
| D | HIS361 |
| site_id | SWS_FT_FI16 |
| 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 | ARG42 | |
| B | ARG42 | |
| C | ARG42 | |
| D | ARG42 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| A | GLU187 | |
| A | LYS229 | |
| A | ASP33 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| B | GLU187 | |
| B | LYS229 | |
| B | ASP33 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| C | GLU187 | |
| C | LYS229 | |
| C | ASP33 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ald |
| Chain | Residue | Details |
| D | GLU187 | |
| D | LYS229 | |
| D | ASP33 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| A | GLU34 | electrostatic stabiliser, hydrogen bond acceptor |
| A | TRP147 | electrostatic stabiliser, hydrogen bond donor |
| A | PRO188 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| A | ILE190 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| A | PRO230 | 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 | TYR301 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| B | GLU34 | electrostatic stabiliser, hydrogen bond acceptor |
| B | TRP147 | electrostatic stabiliser, hydrogen bond donor |
| B | PRO188 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| B | ILE190 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| B | PRO230 | 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 | TYR301 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| C | GLU34 | electrostatic stabiliser, hydrogen bond acceptor |
| C | TRP147 | electrostatic stabiliser, hydrogen bond donor |
| C | PRO188 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| C | ILE190 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| C | PRO230 | 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 | TYR301 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 222 |
| Chain | Residue | Details |
| D | GLU34 | electrostatic stabiliser, hydrogen bond acceptor |
| D | TRP147 | electrostatic stabiliser, hydrogen bond donor |
| D | PRO188 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, polar interaction, proton acceptor, proton donor, proton relay |
| D | ILE190 | activator, electrostatic stabiliser, hydrogen bond acceptor, polar interaction |
| D | PRO230 | 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 | TYR301 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
