2VKR
3Fe-4S, 4Fe-4S plus Zn Acidianus ambivalens ferredoxin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| E | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051536 | molecular_function | iron-sulfur cluster binding |
| F | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| F | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| G | 0008270 | molecular_function | zinc ion binding |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051536 | molecular_function | iron-sulfur cluster binding |
| G | 0051538 | molecular_function | 3 iron, 4 sulfur cluster binding |
| G | 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 F3S A 104 |
| Chain | Residue |
| A | CYS45 |
| A | ILE46 |
| A | ASP48 |
| A | GLY49 |
| A | SER50 |
| A | CYS51 |
| A | CYS93 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 105 |
| Chain | Residue |
| A | CYS83 |
| A | ILE84 |
| A | CYS86 |
| A | MET87 |
| A | CYS89 |
| A | CYS55 |
| A | VAL59 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 106 |
| Chain | Residue |
| A | HIS16 |
| A | HIS19 |
| A | HIS34 |
| A | ASP76 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE F3S B 104 |
| Chain | Residue |
| B | CYS45 |
| B | ILE46 |
| B | ALA47 |
| B | ASP48 |
| B | GLY49 |
| B | SER50 |
| B | CYS51 |
| B | CYS93 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SF4 B 105 |
| Chain | Residue |
| B | CYS55 |
| B | VAL59 |
| B | CYS83 |
| B | CYS86 |
| B | MET87 |
| B | CYS89 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 106 |
| Chain | Residue |
| B | HIS16 |
| B | HIS19 |
| B | HIS34 |
| B | ASP76 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE F3S C 104 |
| Chain | Residue |
| C | CYS45 |
| C | ILE46 |
| C | ASP48 |
| C | GLY49 |
| C | SER50 |
| C | CYS51 |
| C | ALA75 |
| C | CYS93 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 C 105 |
| Chain | Residue |
| C | CYS55 |
| C | VAL59 |
| C | CYS83 |
| C | ILE84 |
| C | CYS86 |
| C | MET87 |
| C | CYS89 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 106 |
| Chain | Residue |
| C | HIS16 |
| C | HIS19 |
| C | HIS34 |
| C | ASP76 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE F3S D 104 |
| Chain | Residue |
| D | CYS45 |
| D | ILE46 |
| D | ALA47 |
| D | ASP48 |
| D | GLY49 |
| D | SER50 |
| D | CYS51 |
| D | ALA75 |
| D | CYS93 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 D 105 |
| Chain | Residue |
| D | CYS55 |
| D | VAL57 |
| D | PHE60 |
| D | CYS83 |
| D | ILE84 |
| D | CYS86 |
| D | MET87 |
| D | CYS89 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 106 |
| Chain | Residue |
| D | HIS16 |
| D | HIS19 |
| D | HIS34 |
| D | ASP76 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE F3S E 104 |
| Chain | Residue |
| E | CYS45 |
| E | ILE46 |
| E | ALA47 |
| E | ASP48 |
| E | GLY49 |
| E | SER50 |
| E | CYS51 |
| E | CYS93 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 E 105 |
| Chain | Residue |
| E | CYS55 |
| E | VAL59 |
| E | CYS83 |
| E | ILE84 |
| E | CYS86 |
| E | MET87 |
| E | CYS89 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN E 106 |
| Chain | Residue |
| E | HIS16 |
| E | HIS19 |
| E | HIS34 |
| E | ASP76 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE F3S F 104 |
| Chain | Residue |
| F | GLY49 |
| F | CYS51 |
| F | CYS93 |
| F | CYS45 |
| F | ILE46 |
| F | ALA47 |
| F | ASP48 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 F 105 |
| Chain | Residue |
| F | CYS55 |
| F | VAL59 |
| F | CYS83 |
| F | ILE84 |
| F | CYS86 |
| F | MET87 |
| F | CYS89 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 106 |
| Chain | Residue |
| F | HIS16 |
| F | HIS19 |
| F | HIS34 |
| F | ASP76 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE F3S G 104 |
| Chain | Residue |
| G | CYS45 |
| G | ILE46 |
| G | ASP48 |
| G | GLY49 |
| G | SER50 |
| G | CYS51 |
| G | ALA75 |
| G | CYS93 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 G 105 |
| Chain | Residue |
| G | CYS55 |
| G | VAL59 |
| G | CYS83 |
| G | ILE84 |
| G | CYS86 |
| G | MET87 |
| G | CYS89 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN G 106 |
| Chain | Residue |
| G | HIS16 |
| G | HIS19 |
| G | HIS34 |
| G | ASP76 |
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. CiFCMaCVnVCP |
| Chain | Residue | Details |
| A | CYS83-PRO94 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 196 |
| 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 | 203 |
| 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 | 245 |
| Details | Region: {"description":"N-terminal extension"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 84 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18258200","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VKR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 14 |
| Details | Modified residue: {"description":"N6-methyllysine; partial","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"499","lastPage":"507","volume":"3","journal":"J. Biol. Inorg. Chem.","title":"Di-cluster, seven iron ferredoxins from hyperthermophilic Sulfolobales.","authors":["Gomes C.M.","Faria A.","Carita J.C.","Mendes J.","Regalla M.","Chicau P.","Huber H.","Stetter K.O.","Teixeira M."]}}]} |
| Chain | Residue | Details |






