1SNN
3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii
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 401 |
| Chain | Residue |
| A | ARG25 |
| A | THR165 |
| A | ILE183 |
| A | GLU185 |
| A | ZN402 |
| A | CA403 |
| A | HOH623 |
| A | HOH668 |
| A | HOH746 |
| A | HOH750 |
| A | HOH751 |
| A | GLU26 |
| A | ASP30 |
| A | CYS55 |
| A | TYR95 |
| A | PHE101 |
| A | ARG161 |
| A | GLY163 |
| A | HIS164 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 5RP B 501 |
| Chain | Residue |
| B | ARG25 |
| B | GLU26 |
| B | ASP30 |
| B | CYS55 |
| B | PHE101 |
| B | ARG161 |
| B | GLY163 |
| B | HIS164 |
| B | THR165 |
| B | GLU185 |
| B | ZN502 |
| B | CA503 |
| B | HOH632 |
| B | HOH664 |
| B | HOH672 |
| B | HOH679 |
| B | HOH686 |
| B | HOH705 |
| B | HOH706 |
| B | HOH707 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | GLU26 |
| A | HIS164 |
| A | 5RP401 |
| A | HOH751 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 403 |
| Chain | Residue |
| A | GLU26 |
| A | TYR95 |
| A | 5RP401 |
| A | HOH668 |
| A | HOH750 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | GLU26 |
| B | HIS164 |
| B | 5RP501 |
| B | HOH706 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| B | GLU26 |
| B | 5RP501 |
| B | HOH664 |
| B | HOH705 |
| B | HOH707 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 601 |
| Chain | Residue |
| A | ASP96 |
| A | GLU97 |
| A | HOH654 |
| A | HOH671 |
| A | HOH676 |
| A | HOH706 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 602 |
| Chain | Residue |
| A | GLU204 |
| A | ASN207 |
| A | HOH688 |
| B | HOH514 |
| B | HOH554 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN A 603 |
| 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 | a catalytic site defined by CSA, PubMed 11827524, 12904291, 12200440 |
| Chain | Residue | Details |
| A | GLU185 | |
| A | ASN106 | |
| A | TYR95 | |
| A | ASP30 | |
| A | SER147 | |
| A | CYS55 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 11827524, 12904291, 12200440 |
| 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) |
