5GK5
Apo structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.9 angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016829 | molecular_function | lyase activity |
A | 0016832 | molecular_function | aldehyde-lyase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016829 | molecular_function | lyase activity |
B | 0016832 | molecular_function | aldehyde-lyase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005829 | cellular_component | cytosol |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0006094 | biological_process | gluconeogenesis |
C | 0006096 | biological_process | glycolytic process |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016829 | molecular_function | lyase activity |
C | 0016832 | molecular_function | aldehyde-lyase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005829 | cellular_component | cytosol |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0006094 | biological_process | gluconeogenesis |
D | 0006096 | biological_process | glycolytic process |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016829 | molecular_function | lyase activity |
D | 0016832 | molecular_function | aldehyde-lyase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005829 | cellular_component | cytosol |
E | 0005975 | biological_process | carbohydrate metabolic process |
E | 0006094 | biological_process | gluconeogenesis |
E | 0006096 | biological_process | glycolytic process |
E | 0008270 | molecular_function | zinc ion binding |
E | 0016829 | molecular_function | lyase activity |
E | 0016832 | molecular_function | aldehyde-lyase activity |
E | 0042802 | molecular_function | identical protein binding |
E | 0042803 | molecular_function | protein homodimerization activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
F | 0005515 | molecular_function | protein binding |
F | 0005829 | cellular_component | cytosol |
F | 0005975 | biological_process | carbohydrate metabolic process |
F | 0006094 | biological_process | gluconeogenesis |
F | 0006096 | biological_process | glycolytic process |
F | 0008270 | molecular_function | zinc ion binding |
F | 0016829 | molecular_function | lyase activity |
F | 0016832 | molecular_function | aldehyde-lyase activity |
F | 0042802 | molecular_function | identical protein binding |
F | 0042803 | molecular_function | protein homodimerization activity |
F | 0046872 | molecular_function | metal ion binding |
G | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
G | 0005515 | molecular_function | protein binding |
G | 0005829 | cellular_component | cytosol |
G | 0005975 | biological_process | carbohydrate metabolic process |
G | 0006094 | biological_process | gluconeogenesis |
G | 0006096 | biological_process | glycolytic process |
G | 0008270 | molecular_function | zinc ion binding |
G | 0016829 | molecular_function | lyase activity |
G | 0016832 | molecular_function | aldehyde-lyase activity |
G | 0042802 | molecular_function | identical protein binding |
G | 0042803 | molecular_function | protein homodimerization activity |
G | 0046872 | molecular_function | metal ion binding |
H | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
H | 0005515 | molecular_function | protein binding |
H | 0005829 | cellular_component | cytosol |
H | 0005975 | biological_process | carbohydrate metabolic process |
H | 0006094 | biological_process | gluconeogenesis |
H | 0006096 | biological_process | glycolytic process |
H | 0008270 | molecular_function | zinc ion binding |
H | 0016829 | molecular_function | lyase activity |
H | 0016832 | molecular_function | aldehyde-lyase activity |
H | 0042802 | molecular_function | identical protein binding |
H | 0042803 | molecular_function | protein homodimerization activity |
H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue GOL A 401 |
Chain | Residue |
A | GLN18 |
A | TYR206 |
A | PRO214 |
A | SER258 |
A | ASN260 |
A | HOH510 |
A | HOH532 |
A | HOH560 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | GLU174 |
A | HIS226 |
A | HIS264 |
A | HOH573 |
A | HIS110 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue ZN A 403 |
Chain | Residue |
A | HIS110 |
A | HIS226 |
A | HIS264 |
A | HOH576 |
A | HOH617 |
A | HOH631 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue GOL B 401 |
Chain | Residue |
B | PRO214 |
B | SER258 |
B | LEU259 |
B | ASN260 |
B | HOH528 |
B | HOH550 |
B | HOH593 |
G | HOH564 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue PEG B 402 |
Chain | Residue |
A | SER88 |
A | HIS91 |
A | HIS92 |
A | GLN95 |
B | SER88 |
B | HIS91 |
B | HIS92 |
B | GLN95 |
B | HOH553 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue ZN B 403 |
Chain | Residue |
B | HIS110 |
B | GLU174 |
B | HIS226 |
B | HIS264 |
B | HOH578 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue GOL C 401 |
Chain | Residue |
C | GLN18 |
C | TYR206 |
C | PRO214 |
C | SER258 |
C | LEU259 |
C | ASN260 |
C | HOH1204 |
C | HOH1225 |
C | HOH1262 |
site_id | AC8 |
Number of Residues | 13 |
Details | binding site for residue PEG C 402 |
Chain | Residue |
C | VAL37 |
C | GLY38 |
C | THR39 |
C | ASP40 |
C | HOH1201 |
C | HOH1207 |
C | HOH1209 |
D | VAL37 |
D | GLY38 |
D | THR39 |
D | ASP40 |
D | HOH524 |
D | HOH541 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue ZN C 403 |
Chain | Residue |
C | HIS110 |
C | GLU174 |
C | HIS226 |
C | HIS264 |
C | HOH1223 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue ZN C 404 |
Chain | Residue |
C | HIS110 |
C | HIS226 |
C | HIS264 |
C | HOH1227 |
C | HOH1308 |
C | HOH1322 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue GOL D 401 |
Chain | Residue |
D | GLN18 |
D | PRO214 |
D | SER258 |
D | LEU259 |
D | HOH508 |
D | HOH516 |
D | HOH585 |
D | HOH606 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue PEG D 402 |
Chain | Residue |
C | SER88 |
C | HIS91 |
C | HIS92 |
C | GLN95 |
D | SER88 |
D | HIS91 |
D | HIS92 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue ZN D 403 |
Chain | Residue |
D | HIS110 |
D | GLU174 |
D | HIS226 |
D | HIS264 |
D | HOH572 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue ZN D 404 |
Chain | Residue |
D | HOH644 |
D | HIS110 |
D | HIS226 |
D | HIS264 |
D | HOH556 |
D | HOH636 |
site_id | AD6 |
Number of Residues | 9 |
Details | binding site for residue GOL E 401 |
Chain | Residue |
E | GLN18 |
E | PRO214 |
E | PHE216 |
E | SER258 |
E | LEU259 |
E | ASN260 |
E | HOH531 |
E | HOH548 |
E | HOH575 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue PEG E 402 |
Chain | Residue |
E | SER88 |
E | HIS91 |
E | HIS92 |
E | GLN95 |
E | HOH585 |
F | SER88 |
F | HIS91 |
F | HIS92 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue ZN E 403 |
Chain | Residue |
E | HIS110 |
E | GLU174 |
E | HIS226 |
E | HIS264 |
E | HOH559 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue ZN E 404 |
Chain | Residue |
E | HIS110 |
E | HIS226 |
E | HIS264 |
E | HOH535 |
E | HOH619 |
E | HOH626 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue ZN F 401 |
Chain | Residue |
F | HIS110 |
F | GLU174 |
F | HIS226 |
F | HIS264 |
F | HOH573 |
site_id | AE2 |
Number of Residues | 7 |
Details | binding site for residue GOL G 401 |
Chain | Residue |
G | GLN18 |
G | PRO214 |
G | SER258 |
G | LEU259 |
G | ASN260 |
G | HOH509 |
G | HOH557 |
site_id | AE3 |
Number of Residues | 15 |
Details | binding site for residue PEG G 402 |
Chain | Residue |
G | VAL37 |
G | GLY38 |
G | THR39 |
G | ASP40 |
G | LEU334 |
G | HOH511 |
G | HOH515 |
H | VAL37 |
H | GLY38 |
H | THR39 |
H | ASP40 |
H | LEU334 |
H | HOH510 |
H | HOH518 |
H | HOH525 |
site_id | AE4 |
Number of Residues | 8 |
Details | binding site for residue PEG G 403 |
Chain | Residue |
G | SER88 |
G | HIS91 |
G | HIS92 |
G | GLN95 |
G | HOH596 |
H | SER88 |
H | HIS91 |
H | HIS92 |
site_id | AE5 |
Number of Residues | 5 |
Details | binding site for residue ZN G 404 |
Chain | Residue |
G | HIS110 |
G | GLU174 |
G | HIS226 |
G | HIS264 |
G | HOH573 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue ZN G 405 |
Chain | Residue |
G | HIS110 |
G | HIS226 |
G | HIS264 |
G | HOH538 |
G | HOH606 |
G | HOH624 |
site_id | AE7 |
Number of Residues | 7 |
Details | binding site for residue GOL H 401 |
Chain | Residue |
H | PRO214 |
H | SER258 |
H | ASN260 |
H | HOH537 |
H | HOH548 |
H | HOH583 |
H | HOH597 |
site_id | AE8 |
Number of Residues | 5 |
Details | binding site for residue ZN H 402 |
Chain | Residue |
H | HIS110 |
H | GLU174 |
H | HIS226 |
H | HIS264 |
H | HOH516 |
site_id | AE9 |
Number of Residues | 6 |
Details | binding site for residue ZN H 403 |
Chain | Residue |
H | HIS110 |
H | HIS226 |
H | HIS264 |
H | HOH531 |
H | HOH627 |
H | HOH631 |
Functional Information from PROSITE/UniProt
site_id | PS00602 |
Number of Residues | 12 |
Details | ALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHC |
Chain | Residue | Details |
A | TYR100-CYS111 |
site_id | PS00806 |
Number of Residues | 12 |
Details | ALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiELGctGGeE |
Chain | Residue | Details |
A | LEU171-GLU182 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:10080900 |
Chain | Residue | Details |
A | ASP109 | |
B | ASP109 | |
C | ASP109 | |
D | ASP109 | |
E | ASP109 | |
F | ASP109 | |
G | ASP109 | |
H | ASP109 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | SER61 | |
B | SER61 | |
C | SER61 | |
D | SER61 | |
E | SER61 | |
F | SER61 | |
G | SER61 | |
H | SER61 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754 |
Chain | Residue | Details |
A | HIS110 | |
B | HIS264 | |
C | HIS110 | |
C | ASP144 | |
C | GLU174 | |
C | HIS226 | |
C | HIS264 | |
D | HIS110 | |
D | ASP144 | |
D | GLU174 | |
D | HIS226 | |
A | ASP144 | |
D | HIS264 | |
E | HIS110 | |
E | ASP144 | |
E | GLU174 | |
E | HIS226 | |
E | HIS264 | |
F | HIS110 | |
F | ASP144 | |
F | GLU174 | |
F | HIS226 | |
A | GLU174 | |
F | HIS264 | |
G | HIS110 | |
G | ASP144 | |
G | GLU174 | |
G | HIS226 | |
G | HIS264 | |
H | HIS110 | |
H | ASP144 | |
H | GLU174 | |
H | HIS226 | |
A | HIS226 | |
H | HIS264 | |
A | HIS264 | |
B | HIS110 | |
B | ASP144 | |
B | GLU174 | |
B | HIS226 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY227 | |
D | GLY227 | |
D | GLY265 | |
D | ASN286 | |
E | GLY227 | |
E | GLY265 | |
E | ASN286 | |
F | GLY227 | |
F | GLY265 | |
F | ASN286 | |
G | GLY227 | |
A | GLY265 | |
G | GLY265 | |
G | ASN286 | |
H | GLY227 | |
H | GLY265 | |
H | ASN286 | |
A | ASN286 | |
B | GLY227 | |
B | GLY265 | |
B | ASN286 | |
C | GLY227 | |
C | GLY265 | |
C | ASN286 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | LYS8 | |
B | LYS8 | |
C | LYS8 | |
D | LYS8 | |
E | LYS8 | |
F | LYS8 | |
G | LYS8 | |
H | LYS8 |
site_id | SWS_FT_FI6 |
Number of Residues | 56 |
Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122 |
Chain | Residue | Details |
A | LYS71 | |
B | LYS230 | |
B | LYS250 | |
B | LYS318 | |
B | LYS325 | |
B | LYS347 | |
C | LYS71 | |
C | LYS114 | |
C | LYS230 | |
C | LYS250 | |
C | LYS318 | |
A | LYS114 | |
C | LYS325 | |
C | LYS347 | |
D | LYS71 | |
D | LYS114 | |
D | LYS230 | |
D | LYS250 | |
D | LYS318 | |
D | LYS325 | |
D | LYS347 | |
E | LYS71 | |
A | LYS230 | |
E | LYS114 | |
E | LYS230 | |
E | LYS250 | |
E | LYS318 | |
E | LYS325 | |
E | LYS347 | |
F | LYS71 | |
F | LYS114 | |
F | LYS230 | |
F | LYS250 | |
A | LYS250 | |
F | LYS318 | |
F | LYS325 | |
F | LYS347 | |
G | LYS71 | |
G | LYS114 | |
G | LYS230 | |
G | LYS250 | |
G | LYS318 | |
G | LYS325 | |
G | LYS347 | |
A | LYS318 | |
H | LYS71 | |
H | LYS114 | |
H | LYS230 | |
H | LYS250 | |
H | LYS318 | |
H | LYS325 | |
H | LYS347 | |
A | LYS325 | |
A | LYS347 | |
B | LYS71 | |
B | LYS114 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
A | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | HIS110 | metal ligand |
A | GLU182 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | HIS226 | metal ligand |
A | HIS264 | metal ligand |
A | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
B | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | HIS110 | metal ligand |
B | GLU182 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | HIS226 | metal ligand |
B | HIS264 | metal ligand |
B | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
C | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | HIS110 | metal ligand |
C | GLU182 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | HIS226 | metal ligand |
C | HIS264 | metal ligand |
C | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
D | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | HIS110 | metal ligand |
D | GLU182 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | HIS226 | metal ligand |
D | HIS264 | metal ligand |
D | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA5 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
E | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
E | HIS110 | metal ligand |
E | GLU182 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
E | HIS226 | metal ligand |
E | HIS264 | metal ligand |
E | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA6 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
F | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
F | HIS110 | metal ligand |
F | GLU182 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
F | HIS226 | metal ligand |
F | HIS264 | metal ligand |
F | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA7 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
G | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
G | HIS110 | metal ligand |
G | GLU182 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
G | HIS226 | metal ligand |
G | HIS264 | metal ligand |
G | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |
site_id | MCSA8 |
Number of Residues | 6 |
Details | M-CSA 52 |
Chain | Residue | Details |
H | ASP109 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
H | HIS110 | metal ligand |
H | GLU182 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
H | HIS226 | metal ligand |
H | HIS264 | metal ligand |
H | ASN286 | electrostatic stabiliser, hydrogen bond donor, steric role |