1PVY
3,4-dihydroxy-2-butanone 4-phosphate synthase from M. jannaschii in complex with ribulose 5-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0030145 | molecular_function | manganese ion binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| 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 | 0030145 | molecular_function | manganese ion binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE 5RP A 501 |
| Chain | Residue |
| A | ARG25 |
| A | THR165 |
| A | ILE183 |
| A | GLU185 |
| A | ZN502 |
| A | CA503 |
| A | HOH723 |
| A | HOH766 |
| A | HOH847 |
| A | HOH851 |
| A | HOH852 |
| A | GLU26 |
| A | ASP30 |
| A | CYS55 |
| A | TYR95 |
| A | LEU151 |
| A | ARG161 |
| A | GLY163 |
| A | HIS164 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 5RP B 601 |
| Chain | Residue |
| B | ARG25 |
| B | GLU26 |
| B | ASP30 |
| B | CYS55 |
| B | PHE101 |
| B | ARG161 |
| B | GLY163 |
| B | HIS164 |
| B | THR165 |
| B | GLU185 |
| B | ZN602 |
| B | CA603 |
| B | HOH772 |
| B | HOH778 |
| B | HOH785 |
| B | HOH804 |
| B | HOH805 |
| B | HOH806 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | GLU26 |
| A | HIS164 |
| A | 5RP501 |
| A | HOH852 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | GLU26 |
| A | TYR95 |
| A | 5RP501 |
| A | HOH851 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 602 |
| Chain | Residue |
| B | GLU26 |
| B | HIS164 |
| B | 5RP601 |
| B | HOH805 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 603 |
| Chain | Residue |
| B | GLU26 |
| B | 5RP601 |
| B | HOH764 |
| B | HOH804 |
| B | HOH806 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 701 |
| Chain | Residue |
| A | ASP96 |
| A | GLU97 |
| A | HOH753 |
| A | HOH769 |
| A | HOH774 |
| A | HOH806 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 702 |
| Chain | Residue |
| A | GLU204 |
| A | ASN207 |
| A | HOH787 |
| B | HOH613 |
| B | HOH655 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN A 703 |
| Chain | Residue |
| A | HIS206 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12904291","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15213409","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PVY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SNN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12904291","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15213409","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1PVY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SNN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Essential for catalytic activity"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1snn |
| Chain | Residue | Details |
| A | GLU185 | |
| A | ASN106 | |
| A | TYR95 | |
| A | ASP30 | |
| A | SER147 | |
| A | CYS55 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1snn |
| Chain | Residue | Details |
| B | GLU185 | |
| B | ASN106 | |
| B | TYR95 | |
| B | ASP30 | |
| B | SER147 | |
| B | CYS55 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 648 |
| Chain | Residue | Details |
| A | ASP30 | proton shuttle (general acid/base) |
| A | CYS55 | proton shuttle (general acid/base) |
| A | TYR95 | electrostatic stabiliser |
| A | ASN106 | electrostatic stabiliser |
| A | SER147 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | GLU185 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 648 |
| Chain | Residue | Details |
| B | ASP30 | proton shuttle (general acid/base) |
| B | CYS55 | proton shuttle (general acid/base) |
| B | TYR95 | electrostatic stabiliser |
| B | ASN106 | electrostatic stabiliser |
| B | SER147 | electrostatic stabiliser, proton shuttle (general acid/base) |
| B | GLU185 | proton shuttle (general acid/base) |
