6CIQ
Pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica with coenzyme A bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005506 | molecular_function | iron ion binding |
| 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 | 0030976 | molecular_function | thiamine pyrophosphate binding |
| 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 | 0003824 | molecular_function | catalytic activity |
| B | 0005506 | molecular_function | iron ion binding |
| 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 | 0030976 | molecular_function | thiamine pyrophosphate binding |
| 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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0006086 | biological_process | pyruvate decarboxylation to acetyl-CoA |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
| C | 0019164 | molecular_function | pyruvate synthase activity |
| C | 0022900 | biological_process | electron transport chain |
| C | 0030976 | molecular_function | thiamine pyrophosphate binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 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 SF4 A 1201 |
| Chain | Residue |
| A | TRP681 |
| A | CYS686 |
| A | ILE687 |
| A | CYS689 |
| A | ASN690 |
| A | CYS692 |
| A | CYS752 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 A 1202 |
| Chain | Residue |
| A | ILE701 |
| A | CYS742 |
| A | THR743 |
| A | CYS745 |
| A | GLY746 |
| A | CYS748 |
| A | PRO679 |
| A | CYS696 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SF4 A 1203 |
| Chain | Residue |
| A | CYS809 |
| A | CYS812 |
| A | GLU814 |
| A | CYS837 |
| A | CYS1075 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue TPP A 1204 |
| Chain | Residue |
| A | PRO27 |
| A | ILE28 |
| A | GLU62 |
| A | GLU814 |
| A | GLY836 |
| A | CYS837 |
| A | PHE866 |
| A | GLU867 |
| A | GLY966 |
| A | ASP967 |
| A | GLY968 |
| A | TRP969 |
| A | THR995 |
| A | VAL997 |
| A | TYR998 |
| A | SER999 |
| A | ASN1000 |
| A | THR1001 |
| A | MG1205 |
| A | HOH1303 |
| A | HOH1310 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 1205 |
| Chain | Residue |
| A | ASP967 |
| A | THR995 |
| A | VAL997 |
| A | TPP1204 |
| A | HOH1303 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue COA A 1206 |
| Chain | Residue |
| A | THR29 |
| A | LEU422 |
| A | GLY423 |
| A | SER424 |
| A | ASP425 |
| A | GLY426 |
| A | THR427 |
| A | VAL428 |
| A | GLY429 |
| A | TYR452 |
| A | THR461 |
| A | ARG554 |
| A | ASN556 |
| A | TYR587 |
| A | ASN598 |
| A | ASN1000 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 B 1201 |
| Chain | Residue |
| B | TRP681 |
| B | CYS686 |
| B | ILE687 |
| B | CYS689 |
| B | ASN690 |
| B | CYS692 |
| B | CYS752 |
| B | LEU759 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 1202 |
| Chain | Residue |
| B | CYS696 |
| B | ILE701 |
| B | CYS742 |
| B | THR743 |
| B | CYS745 |
| B | GLY746 |
| B | CYS748 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SF4 B 1203 |
| Chain | Residue |
| B | CYS809 |
| B | CYS812 |
| B | GLU814 |
| B | CYS837 |
| B | CYS1075 |
| site_id | AD1 |
| Number of Residues | 24 |
| Details | binding site for residue TPP B 1204 |
| Chain | Residue |
| B | TYR998 |
| B | SER999 |
| B | ASN1000 |
| B | THR1001 |
| B | MG1205 |
| B | HOH1301 |
| B | HOH1308 |
| B | PRO27 |
| B | ILE28 |
| B | GLU62 |
| B | GLN86 |
| B | GLU814 |
| B | THR835 |
| B | GLY836 |
| B | CYS837 |
| B | PHE866 |
| B | GLU867 |
| B | GLY966 |
| B | ASP967 |
| B | GLY968 |
| B | TRP969 |
| B | ILE973 |
| B | THR995 |
| B | VAL997 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 1205 |
| Chain | Residue |
| B | ASP967 |
| B | THR995 |
| B | VAL997 |
| B | TPP1204 |
| B | HOH1301 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue COA B 1206 |
| Chain | Residue |
| B | THR29 |
| B | ILE121 |
| B | SER424 |
| B | ASP425 |
| B | GLY426 |
| B | THR427 |
| B | VAL428 |
| B | GLY429 |
| B | LYS456 |
| B | ARG554 |
| B | ASN556 |
| B | TYR587 |
| B | ASN598 |
| B | ASN1000 |
| B | HOH1308 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 C 1201 |
| Chain | Residue |
| C | TRP681 |
| C | CYS686 |
| C | ILE687 |
| C | CYS689 |
| C | ASN690 |
| C | CYS692 |
| C | CYS752 |
| C | ALA758 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 C 1202 |
| Chain | Residue |
| C | CYS696 |
| C | ILE701 |
| C | CYS742 |
| C | THR743 |
| C | CYS745 |
| C | GLY746 |
| C | CYS748 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue SF4 C 1203 |
| Chain | Residue |
| C | LYS456 |
| C | CYS809 |
| C | CYS812 |
| C | GLU814 |
| C | CYS837 |
| C | CYS1075 |
| site_id | AD7 |
| Number of Residues | 23 |
| Details | binding site for residue TPP C 1204 |
| Chain | Residue |
| C | PRO27 |
| C | ILE28 |
| C | GLU62 |
| C | GLN86 |
| C | GLU814 |
| C | GLY836 |
| C | CYS837 |
| C | PHE866 |
| C | GLU867 |
| C | GLY966 |
| C | ASP967 |
| C | GLY968 |
| C | TRP969 |
| C | THR995 |
| C | VAL997 |
| C | TYR998 |
| C | SER999 |
| C | ASN1000 |
| C | THR1001 |
| C | MG1205 |
| C | COA1206 |
| C | HOH1301 |
| C | HOH1303 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 1205 |
| Chain | Residue |
| C | ASP967 |
| C | THR995 |
| C | VAL997 |
| C | TPP1204 |
| C | HOH1301 |
| site_id | AD9 |
| Number of Residues | 21 |
| Details | binding site for residue COA C 1206 |
| Chain | Residue |
| C | THR29 |
| C | ARG112 |
| C | ILE121 |
| C | GLY423 |
| C | SER424 |
| C | ASP425 |
| C | GLY426 |
| C | THR427 |
| C | VAL428 |
| C | TYR452 |
| C | ASP453 |
| C | LYS455 |
| C | LYS456 |
| C | ARG554 |
| C | ASN556 |
| C | VAL557 |
| C | TYR587 |
| C | ASN598 |
| C | ASN1000 |
| C | THR1001 |
| C | TPP1204 |
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. CiQCNqCSlVCP |
| Chain | Residue | Details |
| A | CYS686-PRO697 | |
| A | CYS742-PRO753 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 87 |
| 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 | 93 |
| 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 | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29581263","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6CIO","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29581263","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CIQ","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 66 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29581263","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CIN","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29581263","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CIO","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
