1TKU
Crystal Structure of 3,4-Dihydroxy-2-butanone 4-phosphate Synthase of Candida albicans in complex with Ribulose-5-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0005829 | cellular_component | cytosol |
| A | 0008686 | molecular_function | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity |
| A | 0009231 | biological_process | riboflavin biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0005829 | cellular_component | cytosol |
| B | 0008686 | molecular_function | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity |
| B | 0009231 | biological_process | riboflavin biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 5RP A 701 |
| Chain | Residue |
| A | ASP34 |
| A | HOH803 |
| A | HOH893 |
| A | HOH894 |
| A | HOH915 |
| A | HOH940 |
| A | HOH952 |
| A | HOH972 |
| A | THR85 |
| A | LEU132 |
| A | ARG142 |
| A | GLY144 |
| A | HIS145 |
| A | THR146 |
| A | ILE164 |
| A | GLU166 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5RP B 801 |
| Chain | Residue |
| B | ASP34 |
| B | THR85 |
| B | LEU132 |
| B | ARG142 |
| B | GLY144 |
| B | HIS145 |
| B | THR146 |
| B | ILE164 |
| B | GLU166 |
| B | HOH944 |
| B | HOH970 |
| B | HOH992 |
| B | HOH1005 |
| B | HOH1025 |
| B | HOH1065 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8TG90","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15328619","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TKU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RIU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Essential for catalytic activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Essential for catalytic activity","evidences":[{"source":"PubMed","id":"15328619","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-glutathionyl cysteine","evidences":[{"source":"UniProtKB","id":"Q99258","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1k4l |
| Chain | Residue | Details |
| A | ASP34 | |
| A | GLU166 | |
| A | ASP92 | |
| A | TYR87 | |
| A | CYS59 | |
| A | HIS128 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1k4l |
| Chain | Residue | Details |
| B | ASP34 | |
| B | GLU166 | |
| B | ASP92 | |
| B | TYR87 | |
| B | CYS59 | |
| B | HIS128 |
