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 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ARG25 | |
A | ASP30 | |
A | ARG161 | |
B | ARG25 | |
B | ASP30 | |
B | ARG161 | |
Chain | Residue | Details |
A | GLU26 | |
A | HIS164 | |
B | GLU26 | |
B | HIS164 | |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Essential for catalytic activity |
Chain | Residue | Details |
A | SER147 | |
A | GLU185 | |
B | SER147 | |
B | GLU185 | |
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) |