5FF2
HydE from T. maritima in complex with (2R,4R)-TDA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042364 | biological_process | water-soluble vitamin biosynthetic process |
| A | 0044272 | biological_process | sulfur compound biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue SF4 A 401 |
| Chain | Residue |
| A | CYS63 |
| A | CYS67 |
| A | CYS70 |
| A | SAH408 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue CPS A 402 |
| Chain | Residue |
| A | GLU280 |
| A | ARG284 |
| A | MET324 |
| A | LEU330 |
| A | CPS405 |
| A | CPS406 |
| A | HOH540 |
| A | HOH543 |
| A | HOH561 |
| A | HOH571 |
| A | HOH599 |
| A | HOH657 |
| A | HOH662 |
| A | HOH776 |
| A | GLN98 |
| A | PHE99 |
| A | GLY100 |
| A | PRO276 |
| A | GLY277 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue CPS A 403 |
| Chain | Residue |
| A | LYS37 |
| A | ASP40 |
| A | LYS170 |
| A | ARG284 |
| A | SER297 |
| A | LYS315 |
| A | ASP316 |
| A | THR317 |
| A | HOH603 |
| A | HOH616 |
| A | HOH623 |
| A | HOH648 |
| A | HOH653 |
| A | HOH737 |
| A | HOH803 |
| A | HOH840 |
| A | HOH903 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue CPS A 404 |
| Chain | Residue |
| A | ARG29 |
| A | GLU33 |
| A | THR247 |
| A | CPS405 |
| A | HOH521 |
| A | HOH614 |
| A | HOH615 |
| A | HOH687 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue CPS A 405 |
| Chain | Residue |
| A | ARG29 |
| A | LYS315 |
| A | THR317 |
| A | ALA318 |
| A | CPS402 |
| A | CPS404 |
| A | CPS406 |
| A | HOH626 |
| A | HOH679 |
| A | HOH743 |
| A | HOH755 |
| A | HOH757 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue CPS A 406 |
| Chain | Residue |
| A | LYS128 |
| A | PRO321 |
| A | MET324 |
| A | GLU328 |
| A | CPS402 |
| A | CPS405 |
| A | HOH505 |
| A | HOH551 |
| A | HOH571 |
| A | HOH585 |
| A | HOH597 |
| A | HOH670 |
| A | HOH702 |
| A | HOH721 |
| A | HOH842 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 407 |
| Chain | Residue |
| A | ARG54 |
| A | THR134 |
| A | ARG155 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | binding site for residue SAH A 408 |
| Chain | Residue |
| A | TYR69 |
| A | SER108 |
| A | ARG159 |
| A | GLU161 |
| A | ARG180 |
| A | MET199 |
| A | PRO229 |
| A | ILE231 |
| A | TYR303 |
| A | LEU305 |
| A | TYR306 |
| A | SF4401 |
| A | HOH589 |
| A | HOH608 |
| A | HOH629 |
| A | HOH633 |
| A | HOH739 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue 5XB A 409 |
| Chain | Residue |
| A | THR269 |
| A | ALA270 |
| A | MET291 |
| A | TYR306 |
| A | HOH535 |
| A | HOH547 |
| A | HOH607 |
| A | HOH768 |
| A | HOH800 |
| A | GLN107 |
| A | ARG159 |
| A | GLY226 |
| A | THR268 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue H2S A 410 |
| Chain | Residue |
| A | CYS311 |
| A | CYS319 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue H2S A 411 |
| Chain | Residue |
| A | CYS322 |
| A | HOH915 |
Functional Information from PROSITE/UniProt
| site_id | PS00216 |
| Number of Residues | 18 |
| Details | SUGAR_TRANSPORT_1 Sugar transport proteins signature 1. VMKMIELLGRKpgrdwgG |
| Chain | Residue | Details |
| A | VAL323-GLY340 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 219 |
| Details | Domain: {"description":"Radical SAM core","evidences":[{"source":"PROSITE-ProRule","id":"PRU01266","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PIRSR","id":"PIRSR004762-1","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16137685","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18400755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19706452","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CIX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IIX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PIRSR","id":"PIRSR004762-1","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16137685","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CIW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CIX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IIX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3CIX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3IIZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JXC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JY8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JY9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JYE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3CIX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JY8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JY9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JYE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






