7PLM
CryoEM reconstruction of pyruvate ferredoxin oxidoreductase (PFOR) in anaerobic conditions
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006086 | biological_process | pyruvate decarboxylation to acetyl-CoA |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
| A | 0019164 | molecular_function | pyruvate synthase activity |
| A | 0022900 | biological_process | electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006086 | biological_process | pyruvate decarboxylation to acetyl-CoA |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
| B | 0019164 | molecular_function | pyruvate synthase activity |
| B | 0022900 | biological_process | electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
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. CiQCNqCAfVCP |
| Chain | Residue | Details |
| A | CYS689-PRO700 | |
| A | CYS745-PRO756 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| 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 | 62 |
| 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 | 18 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10048931","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16472741","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10048931","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11752578","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q2RMD6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 58 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10048931","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11752578","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16472741","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"10048931","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 119 |
| Chain | Residue | Details |
| A | THR31 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU64 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG114 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN996 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 119 |
| Chain | Residue | Details |
| B | THR31 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU64 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG114 | electrostatic stabiliser, hydrogen bond donor |
| B | ASN996 | electrostatic stabiliser, hydrogen bond donor |
