8RVV
CryoEM structure of the Elp-Hdr complex of Methanothermobacter marburgensis state 2, dimer (composite structure)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0015948 | biological_process | methanogenesis |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0051912 | molecular_function | CoB--CoM heterodisulfide reductase activity |
| B | 0015948 | biological_process | methanogenesis |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0051912 | molecular_function | CoB--CoM heterodisulfide reductase activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0015948 | biological_process | methanogenesis |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0051912 | molecular_function | CoB--CoM heterodisulfide reductase activity |
| D | 0003954 | molecular_function | NADH dehydrogenase activity |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0022904 | biological_process | respiratory electron transport chain |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0043794 | molecular_function | formate dehydrogenase (coenzyme F420) activity |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0052592 | molecular_function | oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor |
Functional Information from PROSITE/UniProt
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiNCFaCRdACP |
| Chain | Residue | Details |
| E | CYS280-PRO291 | |
| E | CYS330-PRO341 | |
| A | CYS254-PRO265 | |
| A | CYS301-GLU312 | |
| A | CYS591-PRO602 | |
| A | CYS620-PRO631 | |
| C | CYS35-PRO46 | |
| C | CYS79-PRO90 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 60 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 29 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 29 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 23 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
