3OHI
Structure of Giardia fructose-1,6-biphosphate aldolase in complex with 3-hydroxy-2-pyridone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004332 | molecular_function | fructose-bisphosphate aldolase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 340 |
| Chain | Residue |
| A | HIS84 |
| A | HIS178 |
| A | HIS210 |
| A | HDX341 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HDX A 341 |
| Chain | Residue |
| A | GLY179 |
| A | LYS182 |
| A | GLY211 |
| A | SER212 |
| A | SER213 |
| A | ASN253 |
| A | ASP255 |
| A | SER256 |
| A | ARG259 |
| A | ZN340 |
| A | HOH389 |
| B | ARG280 |
| A | ASN24 |
| A | SER50 |
| A | ASP83 |
| A | HIS84 |
| A | HIS178 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 342 |
| Chain | Residue |
| B | HIS84 |
| B | HIS178 |
| B | HIS210 |
| B | HDX343 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HDX B 343 |
| Chain | Residue |
| A | ARG280 |
| B | ASN24 |
| B | GLN48 |
| B | SER50 |
| B | ASP83 |
| B | HIS84 |
| B | HIS178 |
| B | GLY179 |
| B | LYS182 |
| B | GLY211 |
| B | SER212 |
| B | SER213 |
| B | ASN253 |
| B | ASP255 |
| B | SER256 |
| B | ARG259 |
| B | ZN342 |
| B | HOH420 |
Functional Information from PROSITE/UniProt
| site_id | PS00806 |
| Number of Residues | 12 |
| Details | ALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. VEaELGtlGGiE |
| Chain | Residue | Details |
| A | VAL132-GLU143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"19236002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17166851","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19236002","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GAY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GB6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17166851","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19236002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21333622","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ISV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ISW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GAK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GAY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3GB6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OHI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
