5VY5
Rabbit muscle aldolase using 200keV
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 PROSITE/UniProt
site_id | PS00158 |
Number of Residues | 11 |
Details | ALDOLASE_CLASS_I Fructose-bisphosphate aldolase class-I active site. IyLEGtLLKPN |
Chain | Residue | Details |
B | 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 |
B | GLU187 | |
A | 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 |
B | LYS229 | |
A | 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 |
B | ARG42 | |
C | SER271 | |
C | SER300 | |
C | ARG303 | |
D | ARG42 | |
D | SER271 | |
D | SER300 | |
D | ARG303 | |
B | SER271 | |
B | SER300 | |
B | ARG303 | |
A | ARG42 | |
A | SER271 | |
A | SER300 | |
A | ARG303 | |
C | ARG42 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | SITE: Essential for substrate cleavage |
Chain | Residue | Details |
B | CYS72 | |
B | LYS107 | |
A | CYS72 | |
A | 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 |
B | LYS146 | |
A | 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 |
B | HIS361 | |
A | 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 |
B | TYR363 | |
A | 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 |
B | THR8 | |
A | 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 |
B | SER35 | |
C | SER38 | |
C | SER45 | |
C | SER271 | |
D | SER35 | |
D | SER38 | |
D | SER45 | |
D | SER271 | |
B | SER38 | |
B | SER45 | |
B | SER271 | |
A | SER35 | |
A | SER38 | |
A | SER45 | |
A | 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 |
B | LYS41 | |
A | 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 |
B | LYS98 | |
B | LYS146 | |
A | LYS98 | |
A | 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 |
B | LYS107 | |
B | LYS329 | |
A | LYS107 | |
A | 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 |
B | LYS110 | |
A | 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 |
B | SER131 | |
A | SER131 | |
C | SER131 | |
D | SER131 |
site_id | SWS_FT_FI15 |
Number of Residues | 4 |
Details | MOD_RES: N6-malonyllysine => ECO:0000250 |
Chain | Residue | Details |
B | LYS311 | |
A | 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 |
B | ASN360 | |
A | 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 |
B | LYS41 | |
A | LYS41 | |
C | LYS41 | |
D | LYS41 |
Catalytic Information from CSA
site_id | MCSA1 |
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 | MCSA2 |
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 | 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 |