2PU9
Crystal srtucture of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin f
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| 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 |
| A | 0103012 | molecular_function | ferredoxin-thioredoxin reductase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016491 | molecular_function | oxidoreductase activity |
| C | 0015035 | molecular_function | protein-disulfide reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | HIS46 |
| A | LYS63 |
| A | HOH413 |
| A | HOH417 |
| A | HOH418 |
| A | HOH460 |
| A | HOH465 |
| A | HOH509 |
| A | HOH510 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 302 |
| Chain | Residue |
| A | ARG58 |
| B | ASN50 |
| C | ARG87 |
| C | VAL88 |
| C | HOH344 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | ARG45 |
| A | HOH515 |
| C | GLN44 |
| C | TRP45 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | GLU41 |
| A | ARG45 |
| A | LYS113 |
| A | HOH519 |
| B | LYS56 |
| B | ARG60 |
| B | LYS62 |
| B | HOH129 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 305 |
| Chain | Residue |
| A | LYS15 |
| A | ASP96 |
| A | ILE104 |
| A | PRO105 |
| A | MET106 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 306 |
| Chain | Residue |
| C | ALA107 |
| C | TYR109 |
| C | ASP110 |
| C | HOH351 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SF4 A 400 |
| Chain | Residue |
| A | CYS55 |
| A | CYS74 |
| A | CYS76 |
| A | MET79 |
| A | CYS85 |
| A | HIS86 |
| A | CYS87 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10649999","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14769790","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17611542","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19132843","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10649999","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17611542","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Increases the nucleophilicity of the active site Cys","evidences":[{"source":"PubMed","id":"19132843","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Region: {"description":"Interaction with ferredoxin","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Deprotonates C-terminal active site Cys"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Contributes to redox potential value"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cqg |
| Chain | Residue | Details |
| C | CYS46 | |
| C | SER49 |
