6ZMU
Crystal structure of the germline-specific thioredoxin protein Deadhead (Thioredoxin-1) from Drospohila melanogaster, P43212
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0005829 | cellular_component | cytosol |
A | 0007143 | biological_process | female meiotic nuclear division |
A | 0015035 | molecular_function | protein-disulfide reductase activity |
A | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
A | 0035041 | biological_process | sperm DNA decondensation |
A | 0060322 | biological_process | head development |
B | 0005634 | cellular_component | nucleus |
B | 0005829 | cellular_component | cytosol |
B | 0007143 | biological_process | female meiotic nuclear division |
B | 0015035 | molecular_function | protein-disulfide reductase activity |
B | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
B | 0035041 | biological_process | sperm DNA decondensation |
B | 0060322 | biological_process | head development |
C | 0005634 | cellular_component | nucleus |
C | 0005829 | cellular_component | cytosol |
C | 0007143 | biological_process | female meiotic nuclear division |
C | 0015035 | molecular_function | protein-disulfide reductase activity |
C | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
C | 0035041 | biological_process | sperm DNA decondensation |
C | 0060322 | biological_process | head development |
D | 0005634 | cellular_component | nucleus |
D | 0005829 | cellular_component | cytosol |
D | 0007143 | biological_process | female meiotic nuclear division |
D | 0015035 | molecular_function | protein-disulfide reductase activity |
D | 0015038 | molecular_function | glutathione disulfide oxidoreductase activity |
D | 0035041 | biological_process | sperm DNA decondensation |
D | 0060322 | biological_process | head development |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 201 |
Chain | Residue |
A | HOH313 |
C | HOH202 |
D | ARG81 |
D | ARG84 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 202 |
Chain | Residue |
A | THR6 |
A | ASN8 |
A | LYS12 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 203 |
Chain | Residue |
A | ARG68 |
A | TYR69 |
A | TYR10 |
A | HIS11 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 204 |
Chain | Residue |
A | ALA87 |
A | SER88 |
A | HOH301 |
B | ARG68 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue SO4 A 205 |
Chain | Residue |
A | ARG13 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 206 |
Chain | Residue |
A | MET1 |
A | ALA2 |
A | SER3 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue SO4 B 201 |
Chain | Residue |
A | PHE89 |
A | LYS96 |
B | MET7 |
B | TYR10 |
B | HIS11 |
B | LEU65 |
B | ARG68 |
B | HOH303 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 202 |
Chain | Residue |
B | LYS70 |
B | ARG72 |
B | ARG84 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 203 |
Chain | Residue |
A | HIS95 |
B | ARG85 |
B | LEU86 |
B | ALA87 |
B | SER88 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue SO4 B 204 |
Chain | Residue |
A | GLY32 |
A | LYS103 |
B | LYS70 |
B | ARG72 |
B | HOH301 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue NA B 205 |
Chain | Residue |
A | HOH316 |
B | ASP60 |
B | GLU63 |
C | ASP60 |
C | GLU63 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue SO4 D 201 |
Chain | Residue |
D | PHE89 |
D | ALA90 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 202 |
Chain | Residue |
D | MET7 |
D | HIS11 |
D | GLU64 |
D | ARG68 |
D | SO4203 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue SO4 D 203 |
Chain | Residue |
A | ASP19 |
A | GLN82 |
D | TYR10 |
D | HIS11 |
D | ARG68 |
D | TYR69 |
D | SO4202 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue SO4 D 204 |
Chain | Residue |
D | ARG13 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue SO4 D 205 |
Chain | Residue |
B | LYS35 |
D | ARG5 |
D | THR6 |
D | ASN8 |
D | ASP9 |
Functional Information from PROSITE/UniProt
site_id | PS00194 |
Number of Residues | 19 |
Details | THIOREDOXIN_1 Thioredoxin family active site. VLdFYatWCGPCKeMestV |
Chain | Residue | Details |
A | VAL23-VAL41 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | CYS31 | |
A | CYS34 | |
B | CYS31 | |
B | CYS34 | |
C | CYS31 | |
C | CYS34 | |
D | CYS31 | |
D | CYS34 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Deprotonates C-terminal active site Cys => ECO:0000250 |
Chain | Residue | Details |
A | ASP25 | |
B | ASP25 | |
C | ASP25 | |
D | ASP25 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Contributes to redox potential value |
Chain | Residue | Details |
A | GLY32 | |
A | PRO33 | |
B | GLY32 | |
B | PRO33 | |
C | GLY32 | |
C | PRO33 | |
D | GLY32 | |
D | PRO33 |