1XWB
Drospohila thioredoxin, oxidized, P42212
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0006979 | biological_process | response to oxidative stress |
A | 0008340 | biological_process | determination of adult lifespan |
A | 0015035 | molecular_function | protein-disulfide reductase activity |
A | 0015036 | molecular_function | disulfide oxidoreductase activity |
A | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0050832 | biological_process | defense response to fungus |
B | 0005634 | cellular_component | nucleus |
B | 0006979 | biological_process | response to oxidative stress |
B | 0008340 | biological_process | determination of adult lifespan |
B | 0015035 | molecular_function | protein-disulfide reductase activity |
B | 0015036 | molecular_function | disulfide oxidoreductase activity |
B | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
B | 0045454 | biological_process | cell redox homeostasis |
B | 0050832 | biological_process | defense response to fungus |
C | 0005634 | cellular_component | nucleus |
C | 0006979 | biological_process | response to oxidative stress |
C | 0008340 | biological_process | determination of adult lifespan |
C | 0015035 | molecular_function | protein-disulfide reductase activity |
C | 0015036 | molecular_function | disulfide oxidoreductase activity |
C | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
C | 0045454 | biological_process | cell redox homeostasis |
C | 0050832 | biological_process | defense response to fungus |
D | 0005634 | cellular_component | nucleus |
D | 0006979 | biological_process | response to oxidative stress |
D | 0008340 | biological_process | determination of adult lifespan |
D | 0015035 | molecular_function | protein-disulfide reductase activity |
D | 0015036 | molecular_function | disulfide oxidoreductase activity |
D | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
D | 0045454 | biological_process | cell redox homeostasis |
D | 0050832 | biological_process | defense response to fungus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD A 801 |
Chain | Residue |
A | THR30 |
A | ASP61 |
A | HOH830 |
A | HOH854 |
B | GLU64 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD B 802 |
Chain | Residue |
C | HOH137 |
C | HOH142 |
B | GLU88 |
B | HOH845 |
C | GLU88 |
C | HOH117 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD D 803 |
Chain | Residue |
D | GLN48 |
D | GLN48 |
D | PHE49 |
D | PHE49 |
D | GLU99 |
D | GLU99 |
Functional Information from PROSITE/UniProt
site_id | PS00194 |
Number of Residues | 19 |
Details | THIOREDOXIN_1 Thioredoxin family active site. VLdFFatWCGPCKmIspkL |
Chain | Residue | Details |
A | VAL24-LEU42 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q9BRA2 |
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 => ECO:0000250 |
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 => ECO:0000250 |
Chain | Residue | Details |
A | GLY33 | |
A | PRO34 | |
B | GLY33 | |
B | PRO34 | |
C | GLY33 | |
C | PRO34 | |
D | GLY33 | |
D | PRO34 |
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 |