2EIR
Design of Disulfide-linked Thioredoxin Dimers and Multimers Through Analysis of Crystal Contacts
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0030337 | molecular_function | DNA polymerase processivity factor activity |
| A | 0045454 | biological_process | cell redox homeostasis |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0015035 | molecular_function | protein-disulfide reductase activity |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0030337 | molecular_function | DNA polymerase processivity factor activity |
| B | 0045454 | biological_process | cell redox homeostasis |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0015035 | molecular_function | protein-disulfide reductase activity |
| C | 0015036 | molecular_function | disulfide oxidoreductase activity |
| C | 0030337 | molecular_function | DNA polymerase processivity factor activity |
| C | 0045454 | biological_process | cell redox homeostasis |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0015035 | molecular_function | protein-disulfide reductase activity |
| D | 0015036 | molecular_function | disulfide oxidoreductase activity |
| D | 0030337 | molecular_function | DNA polymerase processivity factor activity |
| D | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CU A 201 |
| Chain | Residue |
| A | SER1 |
| A | ASP2 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CU B 1201 |
| Chain | Residue |
| B | SER1 |
| B | ASP2 |
| B | LYS3 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CU C 2201 |
| Chain | Residue |
| C | SER1 |
| C | ASP2 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CU D 3201 |
| Chain | Residue |
| D | SER1 |
| D | ASP2 |
Functional Information from PROSITE/UniProt
| site_id | PS00194 |
| Number of Residues | 19 |
| Details | THIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL |
| Chain | Residue | Details |
| A | LEU24-LEU42 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | CYS32 | |
| A | CYS35 | |
| B | CYS32 | |
| B | CYS35 | |
| C | CYS32 | |
| C | CYS35 | |
| D | CYS32 | |
| D | CYS35 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Deprotonates C-terminal active site Cys |
| Chain | Residue | Details |
| A | ASP26 | |
| B | ASP26 | |
| C | ASP26 | |
| D | ASP26 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | SITE: Contributes to redox potential value |
| Chain | Residue | Details |
| A | GLY33 | |
| A | PRO34 | |
| B | GLY33 | |
| B | PRO34 | |
| C | GLY33 | |
| C | PRO34 | |
| D | GLY33 | |
| D | PRO34 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS69 | |
| B | LYS69 | |
| C | LYS69 | |
| D | LYS69 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| A | PRO34 | |
| A | CYS35 | |
| A | CYS32 | |
| A | GLY33 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| B | PRO34 | |
| B | CYS35 | |
| B | CYS32 | |
| B | GLY33 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| C | PRO34 | |
| C | CYS35 | |
| C | CYS32 | |
| C | GLY33 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| D | PRO34 | |
| D | CYS35 | |
| D | CYS32 | |
| D | GLY33 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| A | CYS35 | |
| A | CYS32 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| B | CYS35 | |
| B | CYS32 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| C | CYS35 | |
| C | CYS32 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| D | CYS35 | |
| D | CYS32 |
