3DXB
Structure of the UHM domain of Puf60 fused to thioredoxin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003723 | molecular_function | RNA 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 | 0045454 | biological_process | cell redox homeostasis |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003723 | molecular_function | RNA 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 | 0045454 | biological_process | cell redox homeostasis |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0003723 | molecular_function | RNA 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 | 0045454 | biological_process | cell redox homeostasis |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0003723 | molecular_function | RNA 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 | 0045454 | biological_process | cell redox homeostasis |
| E | 0003676 | molecular_function | nucleic acid binding |
| E | 0003723 | molecular_function | RNA binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0015035 | molecular_function | protein-disulfide reductase activity |
| E | 0015036 | molecular_function | disulfide oxidoreductase activity |
| E | 0045454 | biological_process | cell redox homeostasis |
| F | 0003676 | molecular_function | nucleic acid binding |
| F | 0003723 | molecular_function | RNA binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0015035 | molecular_function | protein-disulfide reductase activity |
| F | 0015036 | molecular_function | disulfide oxidoreductase activity |
| F | 0045454 | biological_process | cell redox homeostasis |
| G | 0003676 | molecular_function | nucleic acid binding |
| G | 0003723 | molecular_function | RNA binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0015035 | molecular_function | protein-disulfide reductase activity |
| G | 0015036 | molecular_function | disulfide oxidoreductase activity |
| G | 0045454 | biological_process | cell redox homeostasis |
| H | 0003676 | molecular_function | nucleic acid binding |
| H | 0003723 | molecular_function | RNA binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0015035 | molecular_function | protein-disulfide reductase activity |
| H | 0015036 | molecular_function | disulfide oxidoreductase activity |
| H | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1 |
| Chain | Residue |
| A | HIS350 |
| A | TRP372 |
| A | HOH695 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO E 557 |
| Chain | Residue |
| E | ARG464 |
| E | TYR544 |
| E | ASP545 |
| E | ALA556 |
| E | HOH672 |
Functional Information from PROSITE/UniProt
| site_id | PS00194 |
| Number of Residues | 19 |
| Details | THIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL |
| Chain | Residue | Details |
| A | LEU368-LEU386 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | ACT_SITE: Nucleophile => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS376 | |
| E | CYS379 | |
| F | CYS376 | |
| F | CYS379 | |
| G | CYS376 | |
| G | CYS379 | |
| H | CYS376 | |
| H | CYS379 | |
| A | CYS379 | |
| B | CYS376 | |
| B | CYS379 | |
| C | CYS376 | |
| C | CYS379 | |
| D | CYS376 | |
| D | CYS379 | |
| E | CYS376 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | SITE: Deprotonates C-terminal active site Cys => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP370 | |
| B | ASP370 | |
| C | ASP370 | |
| D | ASP370 | |
| E | ASP370 | |
| F | ASP370 | |
| G | ASP370 | |
| H | ASP370 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | SITE: Contributes to redox potential value => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY377 | |
| E | PRO378 | |
| F | GLY377 | |
| F | PRO378 | |
| G | GLY377 | |
| G | PRO378 | |
| H | GLY377 | |
| H | PRO378 | |
| A | PRO378 | |
| B | GLY377 | |
| B | PRO378 | |
| C | GLY377 | |
| C | PRO378 | |
| D | GLY377 | |
| D | PRO378 | |
| E | GLY377 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS413 | |
| B | LYS413 | |
| C | LYS413 | |
| D | LYS413 | |
| E | LYS413 | |
| F | LYS413 | |
| G | LYS413 | |
| H | LYS413 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| A | GLY377 | |
| A | CYS376 | |
| A | CYS379 | |
| A | PRO378 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| B | CYS376 | |
| B | CYS379 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| C | CYS376 | |
| C | CYS379 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| D | CYS376 | |
| D | CYS379 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| E | CYS376 | |
| E | CYS379 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| F | CYS376 | |
| F | CYS379 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| G | CYS376 | |
| G | CYS379 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| H | CYS376 | |
| H | CYS379 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| B | GLY377 | |
| B | CYS376 | |
| B | CYS379 | |
| B | PRO378 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| C | GLY377 | |
| C | CYS376 | |
| C | CYS379 | |
| C | PRO378 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| D | GLY377 | |
| D | CYS376 | |
| D | CYS379 | |
| D | PRO378 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| E | GLY377 | |
| E | CYS376 | |
| E | CYS379 | |
| E | PRO378 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| F | GLY377 | |
| F | CYS376 | |
| F | CYS379 | |
| F | PRO378 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| G | GLY377 | |
| G | CYS376 | |
| G | CYS379 | |
| G | PRO378 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| H | GLY377 | |
| H | CYS376 | |
| H | CYS379 | |
| H | PRO378 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1mek |
| Chain | Residue | Details |
| A | CYS376 | |
| A | CYS379 |
