7C3F
Crystal structure of ferredoxin: thioredoxin reductase and thioredoxin m2 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| B | 0015979 | biological_process | photosynthesis |
| C | 0015035 | molecular_function | protein-disulfide reductase activity |
| D | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| E | 0015979 | biological_process | photosynthesis |
| F | 0015035 | molecular_function | protein-disulfide reductase activity |
| G | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| H | 0015979 | biological_process | photosynthesis |
| I | 0015035 | molecular_function | protein-disulfide reductase activity |
| J | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| K | 0015979 | biological_process | photosynthesis |
| L | 0015035 | molecular_function | protein-disulfide reductase activity |
| M | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| N | 0015979 | biological_process | photosynthesis |
| O | 0015035 | molecular_function | protein-disulfide reductase activity |
| P | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| Q | 0015979 | biological_process | photosynthesis |
| R | 0015035 | molecular_function | protein-disulfide reductase activity |
| S | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| T | 0015979 | biological_process | photosynthesis |
| U | 0015035 | molecular_function | protein-disulfide reductase activity |
| V | 0016730 | molecular_function | oxidoreductase activity, acting on iron-sulfur proteins as donors |
| W | 0015035 | molecular_function | protein-disulfide reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 A 201 |
| Chain | Residue |
| A | CYS54 |
| A | CYS73 |
| A | CYS75 |
| A | MET78 |
| A | CYS84 |
| A | HIS85 |
| A | CYS86 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 202 |
| Chain | Residue |
| A | THR35 |
| A | MET87 |
| A | LEU88 |
| A | PHE28 |
| A | CYS29 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue NA C 201 |
| Chain | Residue |
| C | SER16 |
| C | THR17 |
| C | SER20 |
| D | MET115 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 D 201 |
| Chain | Residue |
| D | CYS54 |
| D | CYS73 |
| D | CYS75 |
| D | MET78 |
| D | CYS84 |
| D | HIS85 |
| D | CYS86 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA D 202 |
| Chain | Residue |
| D | PHE28 |
| D | CYS29 |
| D | THR35 |
| D | MET87 |
| D | LEU88 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NA E 201 |
| Chain | Residue |
| E | VAL46 |
| E | TYR47 |
| E | HIS48 |
| E | VAL49 |
| E | VAL52 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 G 201 |
| Chain | Residue |
| G | CYS54 |
| G | CYS73 |
| G | CYS75 |
| G | MET78 |
| G | CYS84 |
| G | HIS85 |
| G | CYS86 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NA G 202 |
| Chain | Residue |
| G | PHE28 |
| G | CYS29 |
| G | THR35 |
| G | MET87 |
| G | LEU88 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 J 201 |
| Chain | Residue |
| J | CYS54 |
| J | CYS73 |
| J | CYS75 |
| J | MET78 |
| J | CYS84 |
| J | HIS85 |
| J | CYS86 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue NA J 202 |
| Chain | Residue |
| J | PHE28 |
| J | CYS29 |
| J | THR35 |
| J | MET87 |
| J | LEU88 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NA L 201 |
| Chain | Residue |
| L | ASP15 |
| L | SER16 |
| L | TRP18 |
| L | ASP19 |
| O | HOH310 |
| O | HOH347 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 M 201 |
| Chain | Residue |
| M | CYS54 |
| M | CYS73 |
| M | CYS75 |
| M | MET78 |
| M | CYS84 |
| M | HIS85 |
| M | CYS86 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue NA M 202 |
| Chain | Residue |
| M | PHE28 |
| M | CYS29 |
| M | THR35 |
| M | MET87 |
| M | LEU88 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue NA O 201 |
| Chain | Residue |
| M | HIS58 |
| O | THR66 |
| O | ASP67 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 P 201 |
| Chain | Residue |
| P | CYS54 |
| P | CYS73 |
| P | CYS75 |
| P | MET78 |
| P | CYS84 |
| P | HIS85 |
| P | CYS86 |
| P | HOH312 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue NA P 202 |
| Chain | Residue |
| P | ARG57 |
| P | HIS58 |
| Q | SER77 |
| R | ARG79 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 S 201 |
| Chain | Residue |
| S | CYS54 |
| S | CYS73 |
| S | CYS75 |
| S | MET78 |
| S | CYS84 |
| S | HIS85 |
| S | CYS86 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q55389","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33015914","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7BZK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7C2B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7C3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Site: {"description":"Increases the nucleophilicity of the active site Cys","evidences":[{"source":"UniProtKB","id":"Q55389","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Site: {"description":"Deprotonates C-terminal active site Cys","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Site: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






