1GX7
Best model of the electron transfer complex between cytochrome c3 and [Fe]-hydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| D | 0008901 | molecular_function | ferredoxin hydrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0009061 | biological_process | anaerobic respiration |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 A 5 |
| Chain | Residue |
| A | PDT4 |
| A | FE26 |
| A | CYN7 |
| A | CYN8 |
| A | CMO9 |
| A | CMO10 |
| A | MET232 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE2 A 6 |
| Chain | Residue |
| A | CYN7 |
| A | CYN8 |
| A | CMO9 |
| A | CMO10 |
| A | MET232 |
| A | PDT4 |
| A | FE25 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CYN A 7 |
| Chain | Residue |
| A | PDT4 |
| A | FE25 |
| A | FE26 |
| A | CYN8 |
| A | CMO9 |
| A | CMO10 |
| A | PRO203 |
| A | ILE204 |
| A | MET232 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CYN A 8 |
| Chain | Residue |
| A | PDT4 |
| A | FE25 |
| A | FE26 |
| A | CYN7 |
| A | CMO9 |
| A | CMO10 |
| A | ALA107 |
| A | PRO108 |
| A | ALA109 |
| A | MET232 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SF4 A 1 |
| Chain | Residue |
| A | LYS34 |
| A | CYS35 |
| A | ILE36 |
| A | CYS38 |
| A | ASP39 |
| A | CYS41 |
| A | SER42 |
| A | HIS58 |
| A | HIS75 |
| A | CYS76 |
| A | ILE81 |
| E | HEC109 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 2 |
| Chain | Residue |
| A | TYR44 |
| A | CYS45 |
| A | ILE50 |
| A | ALA65 |
| A | CYS66 |
| A | ILE67 |
| A | CYS69 |
| A | GLY70 |
| A | CYS72 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A 3 |
| Chain | Residue |
| A | CYS69 |
| A | CYS179 |
| A | PRO180 |
| A | CYS234 |
| A | MET376 |
| A | ALA377 |
| A | CYS378 |
| A | CYS382 |
| A | GLY385 |
| A | GLY386 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PDT A 4 |
| Chain | Residue |
| A | FE25 |
| A | FE26 |
| A | CYN7 |
| A | CYN8 |
| A | CMO9 |
| A | CMO10 |
| A | PRO203 |
| A | PHE296 |
| A | GLY297 |
| A | MET376 |
| A | CYS382 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CMO A 9 |
| Chain | Residue |
| A | PDT4 |
| A | FE25 |
| A | FE26 |
| A | CYN7 |
| A | CYN8 |
| A | CMO10 |
| A | MET232 |
| A | PRO233 |
| A | LYS237 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CMO A 10 |
| Chain | Residue |
| A | PDT4 |
| A | FE25 |
| A | FE26 |
| A | CYN7 |
| A | CYN8 |
| A | CMO9 |
| A | PRO108 |
| A | THR145 |
| A | MET232 |
| site_id | BC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC E 109 |
| Chain | Residue |
| E | ALA13 |
| E | THR14 |
| E | LYS15 |
| E | GLN16 |
| E | VAL18 |
| E | TYR65 |
| E | HIS70 |
| E | CYS79 |
| E | VAL80 |
| E | LEU97 |
| E | CYS100 |
| E | CYS105 |
| E | HIS106 |
| A | SF41 |
| A | ILE36 |
| A | CYS38 |
| A | MET54 |
| E | MET11 |
| E | GLU12 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC E 110 |
| Chain | Residue |
| E | HIS34 |
| E | HIS35 |
| E | PRO36 |
| E | VAL37 |
| E | ASN38 |
| E | ASP42 |
| E | CYS46 |
| E | THR48 |
| E | CYS51 |
| E | HIS52 |
| E | SER61 |
| E | ALA62 |
| E | HIS67 |
| E | VAL68 |
| E | THR74 |
| E | LYS75 |
| E | PHE76 |
| site_id | BC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEC E 111 |
| Chain | Residue |
| E | PRO2 |
| E | LYS3 |
| E | ALA4 |
| E | PHE20 |
| E | HIS22 |
| E | HIS25 |
| E | LYS26 |
| E | CYS30 |
| E | CYS33 |
| E | HIS34 |
| E | ARG44 |
| E | LYS45 |
| E | CYS46 |
| E | GLY47 |
| E | HEC112 |
| site_id | BC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEC E 112 |
| Chain | Residue |
| E | VAL19 |
| E | PHE20 |
| E | ASN21 |
| E | SER23 |
| E | THR24 |
| E | HIS25 |
| E | CYS33 |
| E | MET69 |
| E | CYS79 |
| E | CYS82 |
| E | HIS83 |
| E | LYS104 |
| E | CYS105 |
| E | HEC111 |
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. CiGCDtCSqYCP |
| Chain | Residue | Details |
| A | CYS35-PRO46 | |
| A | CYS66-PRO77 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| E | HIS22 | |
| A | CYS234 | |
| A | CYS378 | |
| A | CYS382 | |
| E | HIS25 | |
| E | HIS34 | |
| E | HIS35 | |
| E | HIS52 | |
| E | HIS70 | |
| E | HIS83 | |
| E | HIS106 | |
| A | CYS179 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: covalent |
| Chain | Residue | Details |
| E | CYS30 | |
| E | CYS33 | |
| E | CYS46 | |
| E | CYS51 | |
| E | CYS79 | |
| E | CYS82 | |
| E | CYS100 | |
| E | CYS105 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hfe |
| Chain | Residue | Details |
| A | LYS237 | |
| A | CYS178 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 127 |
| Chain | Residue | Details |
| A | GLU156 | proton acceptor, proton donor, proton relay |
| A | GLU159 | proton acceptor, proton donor, proton relay |
| A | CYS178 | proton acceptor, proton donor, proton relay |
| A | SER198 | proton acceptor, proton donor, proton relay |
| A | LYS237 | proton acceptor, proton donor, proton relay |
| A | GLU240 | proton acceptor, proton donor, proton relay |
| A | GLU245 | proton acceptor, proton donor, proton relay |
| A | CYS382 | metal ligand |
