3CIW
X-RAY structure of the [FeFe]-hydrogenase maturase HydE from thermotoga maritima
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 | 7 |
| Details | BINDING SITE FOR RESIDUE CL A 349 |
| Chain | Residue |
| A | ARG159 |
| A | THR268 |
| A | THR269 |
| A | ALA270 |
| A | TYR306 |
| A | HOH2811 |
| A | HOH2812 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 350 |
| Chain | Residue |
| A | ARG155 |
| A | ARG54 |
| A | THR134 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 351 |
| Chain | Residue |
| A | ARG159 |
| A | PRO266 |
| A | MET291 |
| A | HOH2603 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SF4 A 2460 |
| Chain | Residue |
| A | CYS63 |
| A | CYS67 |
| A | CYS70 |
| A | GLY109 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE SAH A 1501 |
| Chain | Residue |
| A | TYR69 |
| A | SER108 |
| A | SER136 |
| A | ARG159 |
| A | GLU161 |
| A | ARG180 |
| A | MET199 |
| A | PRO229 |
| A | ILE231 |
| A | TYR303 |
| A | LEU305 |
| A | HOH2471 |
| A | HOH2477 |
| A | HOH2479 |
| A | HOH2488 |
| A | HOH2527 |
| A | HOH2794 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE CPS A 1701 |
| Chain | Residue |
| A | GLN98 |
| A | PHE99 |
| A | GLY100 |
| A | PRO276 |
| A | GLY277 |
| A | GLU280 |
| A | ARG284 |
| A | MET324 |
| A | LEU330 |
| A | HOH2468 |
| A | HOH2504 |
| A | HOH2554 |
| A | HOH2565 |
| A | HOH2685 |
| A | HOH2753 |
| A | HOH2773 |
| A | HOH2820 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SAT A 1706 |
| Chain | Residue |
| A | LYS170 |
| A | SER297 |
| A | ASP316 |
| A | HOH2781 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CPS A 1702 |
| Chain | Residue |
| A | LYS37 |
| A | ASP40 |
| A | ARG284 |
| A | THR317 |
| A | HOH2558 |
| A | HOH2607 |
| A | HOH2634 |
| A | HOH2653 |
| A | HOH2659 |
| A | HOH2781 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CPS A 1703 |
| Chain | Residue |
| A | ARG29 |
| A | GLU33 |
| A | PHE246 |
| A | THR247 |
| A | LEU250 |
| A | HOH2553 |
| A | HOH2557 |
| A | HOH2563 |
| A | HOH2758 |
| A | HOH2775 |
| A | HOH2824 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CPS A 1704 |
| Chain | Residue |
| A | ARG29 |
| A | THR317 |
| A | ALA318 |
| A | HOH2563 |
| A | HOH2591 |
| A | HOH2688 |
| A | HOH2821 |
| A | HOH2835 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CPS A 1705 |
| Chain | Residue |
| A | LYS128 |
| A | MET324 |
| A | LYS325 |
| A | GLU328 |
| A | HOH2667 |
| A | HOH2703 |
| A | HOH2741 |
| A | HOH2742 |
| A | HOH2773 |
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 | 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_FI2 |
| 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_FI3 |
| 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_FI4 |
| 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 |






