2QUT
Dihydroxyacetone phosphate enamine intermediate in 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 | 13 |
| Details | BINDING SITE FOR RESIDUE 13P A 3001 |
| Chain | Residue |
| A | ALA31 |
| A | ARG303 |
| A | HOH3071 |
| A | HOH3088 |
| A | HOH3415 |
| A | ASP33 |
| A | LYS146 |
| A | LYS229 |
| A | SER271 |
| A | GLY272 |
| A | SER300 |
| A | TYR301 |
| A | GLY302 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 13P B 3002 |
| Chain | Residue |
| B | ALA31 |
| B | ASP33 |
| B | LYS146 |
| B | LYS229 |
| B | LEU270 |
| B | SER271 |
| B | GLY272 |
| B | SER300 |
| B | TYR301 |
| B | GLY302 |
| B | ARG303 |
| B | HOH3051 |
| B | HOH3392 |
| B | HOH3528 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 13P C 3003 |
| Chain | Residue |
| C | ALA31 |
| C | ASP33 |
| C | LYS146 |
| C | LYS229 |
| C | LEU270 |
| C | SER271 |
| C | GLY272 |
| C | SER300 |
| C | TYR301 |
| C | GLY302 |
| C | ARG303 |
| C | HOH3093 |
| C | HOH3175 |
| C | HOH3467 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 13P D 3004 |
| Chain | Residue |
| D | ALA31 |
| D | ASP33 |
| D | LYS146 |
| D | LYS229 |
| D | SER271 |
| D | GLY272 |
| D | SER300 |
| D | GLY302 |
| D | ARG303 |
| D | HOH3042 |
| D | HOH3164 |
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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11779856","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Schiff-base intermediate with dihydroxyacetone-P","evidences":[{"source":"PubMed","id":"11779856","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10504235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ALD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Site: {"description":"Essential for substrate cleavage"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Alkylation inactivates the enzyme"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Site: {"description":"Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Site: {"description":"Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P05065","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Deamidated asparagine; in form beta","evidences":[{"source":"PubMed","id":"4857186","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P04075","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 | 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 | 6 |
| 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 |
