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 | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 96 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
