3QM3
1.85 Angstrom Resolution Crystal Structure of Fructose-bisphosphate Aldolase (Fba) from Campylobacter jejuni
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
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 | 0046872 | molecular_function | metal ion binding |
B | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
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 | 0046872 | molecular_function | metal ion binding |
C | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
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 | 0046872 | molecular_function | metal ion binding |
D | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
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 | 0046872 | molecular_function | metal ion binding |
E | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
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 | 0046872 | molecular_function | metal ion binding |
F | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
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 | 0046872 | molecular_function | metal ion binding |
G | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
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 | 0046872 | molecular_function | metal ion binding |
H | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
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 | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 355 |
Chain | Residue |
A | HIS105 |
A | GLU169 |
A | HIS221 |
A | HIS260 |
A | HOH362 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 356 |
Chain | Residue |
A | HOH2887 |
A | GLY10 |
A | VAL11 |
A | HIS89 |
A | HOH2006 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 357 |
Chain | Residue |
A | LYS86 |
A | HIS128 |
A | HOH2539 |
A | HOH2806 |
B | LYS86 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 358 |
Chain | Residue |
A | GLY261 |
A | GLY262 |
A | SER263 |
A | ASN282 |
A | ILE283 |
A | ASP284 |
A | THR285 |
A | HOH1366 |
A | HOH1552 |
A | HOH3395 |
A | HOH3504 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 355 |
Chain | Residue |
B | HIS105 |
B | GLU169 |
B | HIS221 |
B | HIS260 |
B | HOH2086 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 356 |
Chain | Residue |
B | GLY10 |
B | VAL11 |
B | HIS89 |
B | TYR124 |
B | HOH1484 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GOL B 357 |
Chain | Residue |
B | ASN282 |
B | ILE283 |
B | ASP284 |
B | THR285 |
B | HOH1066 |
B | HOH1533 |
B | HOH1794 |
B | HOH1936 |
B | HOH2194 |
B | HOH2637 |
B | HOH3600 |
B | HOH3601 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 358 |
Chain | Residue |
A | ARG327 |
A | HOH1263 |
B | SER61 |
B | HOH520 |
B | HOH1614 |
B | HOH1796 |
B | HOH1965 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 359 |
Chain | Residue |
A | SER61 |
A | HOH3479 |
B | ARG327 |
B | HOH385 |
B | HOH1328 |
B | HOH3219 |
B | HOH3553 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 360 |
Chain | Residue |
A | ARG331 |
A | GLU335 |
B | LYS71 |
B | ASN72 |
G | LYS109 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 355 |
Chain | Residue |
C | HIS105 |
C | GLU169 |
C | HIS221 |
C | HIS260 |
C | HOH371 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 356 |
Chain | Residue |
C | GLY10 |
C | VAL11 |
C | HIS89 |
C | HOH2502 |
C | HOH2960 |
C | HOH3374 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 C 357 |
Chain | Residue |
C | ARG327 |
C | HOH400 |
C | HOH891 |
C | HOH1374 |
C | HOH1945 |
D | SER61 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 C 358 |
Chain | Residue |
C | SER61 |
C | HOH408 |
C | HOH922 |
C | HOH1865 |
C | HOH3280 |
C | HOH3602 |
D | ARG327 |
site_id | BC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 C 359 |
Chain | Residue |
C | HOH1461 |
C | HOH2299 |
C | HOH3131 |
C | GLY261 |
C | GLY262 |
C | SER263 |
C | ASN282 |
C | ILE283 |
C | ASP284 |
C | THR285 |
C | HOH1252 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 355 |
Chain | Residue |
D | HIS105 |
D | GLU169 |
D | HIS221 |
D | HIS260 |
D | HOH375 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL D 356 |
Chain | Residue |
D | SER263 |
D | ILE283 |
D | ASP284 |
D | THR285 |
D | ASP286 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT D 357 |
Chain | Residue |
D | GLY10 |
D | VAL11 |
D | HIS89 |
D | GLN130 |
D | HOH1874 |
site_id | CC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FMT D 358 |
Chain | Residue |
D | THR285 |
D | SO4360 |
D | HOH2054 |
D | HOH3154 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 359 |
Chain | Residue |
C | ARG331 |
C | GLU335 |
D | LYS71 |
D | ASN72 |
D | HOH3096 |
E | LYS109 |
site_id | CC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 D 360 |
Chain | Residue |
D | SER263 |
D | ASN282 |
D | ILE283 |
D | ASP284 |
D | THR285 |
D | FMT358 |
D | HOH1240 |
D | HOH1540 |
D | HOH2249 |
D | HOH3599 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 355 |
Chain | Residue |
E | HIS105 |
E | GLU169 |
E | HIS221 |
E | HIS260 |
E | HOH367 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL E 356 |
Chain | Residue |
E | GLY10 |
E | VAL11 |
E | HIS89 |
E | HOH1481 |
E | HOH2386 |
E | HOH2674 |
site_id | CC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 E 357 |
Chain | Residue |
E | ARG327 |
E | HOH376 |
E | HOH821 |
E | HOH1871 |
E | HOH2383 |
E | HOH3548 |
F | SER61 |
F | HOH1301 |
site_id | CC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 E 358 |
Chain | Residue |
E | SER61 |
E | ASN62 |
E | GLY63 |
E | HOH1392 |
E | HOH1777 |
E | HOH2196 |
E | HOH2558 |
F | ARG327 |
site_id | CC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 E 359 |
Chain | Residue |
E | GLY261 |
E | GLY262 |
E | SER263 |
E | ASN282 |
E | ILE283 |
E | ASP284 |
E | THR285 |
E | HOH1245 |
E | HOH1505 |
E | HOH1831 |
E | HOH2147 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 360 |
Chain | Residue |
E | HIS128 |
E | HOH3581 |
F | LYS86 |
site_id | DC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 355 |
Chain | Residue |
F | HIS105 |
F | GLU169 |
F | HIS221 |
F | HIS260 |
F | HOH2367 |
site_id | DC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT F 356 |
Chain | Residue |
F | GLY10 |
F | VAL11 |
F | HIS89 |
F | GLN130 |
F | HOH2298 |
F | HOH2416 |
F | HOH3337 |
site_id | DC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL F 357 |
Chain | Residue |
F | GLY261 |
F | SER263 |
F | ASN282 |
F | ILE283 |
F | ASP284 |
F | THR285 |
F | HOH2103 |
F | HOH3186 |
F | HOH3191 |
F | HOH3596 |
site_id | DC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 F 358 |
Chain | Residue |
C | LYS109 |
E | ARG331 |
E | GLU335 |
F | LYS71 |
F | ASN72 |
site_id | DC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN G 355 |
Chain | Residue |
G | HIS105 |
G | GLU169 |
G | HIS221 |
G | HIS260 |
G | HOH379 |
site_id | DC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 G 356 |
Chain | Residue |
G | ARG327 |
G | HOH408 |
G | HOH1222 |
G | HOH1296 |
G | HOH1897 |
G | HOH2443 |
H | SER61 |
H | HOH1901 |
site_id | DC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 G 357 |
Chain | Residue |
G | GLY261 |
G | GLY262 |
G | SER263 |
G | ASN282 |
G | ILE283 |
G | ASP284 |
G | THR285 |
G | HOH1405 |
G | HOH2072 |
G | HOH3512 |
site_id | DC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 G 358 |
Chain | Residue |
G | LYS86 |
G | HIS128 |
G | HOH3554 |
H | LYS86 |
site_id | DC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 G 359 |
Chain | Residue |
G | GLY10 |
G | VAL11 |
G | HIS89 |
G | LYS93 |
G | GLN130 |
G | HOH1682 |
G | HOH2258 |
G | HOH3542 |
site_id | EC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN H 355 |
Chain | Residue |
H | HIS105 |
H | GLU169 |
H | HIS221 |
H | HIS260 |
H | HOH504 |
site_id | EC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT H 356 |
Chain | Residue |
H | GLY10 |
H | VAL11 |
H | HIS89 |
H | HOH1934 |
H | HOH3256 |
site_id | EC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 H 357 |
Chain | Residue |
G | SER61 |
H | ARG327 |
H | HOH369 |
H | HOH377 |
site_id | EC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 H 358 |
Chain | Residue |
A | LYS109 |
G | ARG331 |
G | GLU335 |
H | LYS71 |
H | ASN72 |
H | HOH3257 |
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.LHtDHA |
Chain | Residue | Details |
A | TYR95-ALA106 |
site_id | PS00806 |
Number of Residues | 12 |
Details | ALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiELGctGGeE |
Chain | Residue | Details |
A | LEU166-GLU177 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | ASP104 | |
B | ASP104 | |
C | ASP104 | |
D | ASP104 | |
E | ASP104 | |
F | ASP104 | |
G | ASP104 | |
H | ASP104 |
site_id | SWS_FT_FI2 |
Number of Residues | 72 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | SER61 | |
B | SER61 | |
B | HIS105 | |
B | ASP139 | |
B | GLU169 | |
B | HIS221 | |
B | GLY222 | |
B | HIS260 | |
B | GLY261 | |
B | ASN282 | |
C | SER61 | |
A | HIS105 | |
C | HIS105 | |
C | ASP139 | |
C | GLU169 | |
C | HIS221 | |
C | GLY222 | |
C | HIS260 | |
C | GLY261 | |
C | ASN282 | |
D | SER61 | |
D | HIS105 | |
A | ASP139 | |
D | ASP139 | |
D | GLU169 | |
D | HIS221 | |
D | GLY222 | |
D | HIS260 | |
D | GLY261 | |
D | ASN282 | |
E | SER61 | |
E | HIS105 | |
E | ASP139 | |
A | GLU169 | |
E | GLU169 | |
E | HIS221 | |
E | GLY222 | |
E | HIS260 | |
E | GLY261 | |
E | ASN282 | |
F | SER61 | |
F | HIS105 | |
F | ASP139 | |
F | GLU169 | |
A | HIS221 | |
F | HIS221 | |
F | GLY222 | |
F | HIS260 | |
F | GLY261 | |
F | ASN282 | |
G | SER61 | |
G | HIS105 | |
G | ASP139 | |
G | GLU169 | |
G | HIS221 | |
A | GLY222 | |
G | GLY222 | |
G | HIS260 | |
G | GLY261 | |
G | ASN282 | |
H | SER61 | |
H | HIS105 | |
H | ASP139 | |
H | GLU169 | |
H | HIS221 | |
H | GLY222 | |
A | HIS260 | |
H | HIS260 | |
H | GLY261 | |
H | ASN282 | |
A | GLY261 | |
A | ASN282 |