4Y4L
Crystal structure of yeast Thi4-C205S
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000002 | biological_process | mitochondrial genome maintenance |
A | 0005506 | molecular_function | iron ion binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008198 | molecular_function | ferrous iron binding |
A | 0009228 | biological_process | thiamine biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0052837 | biological_process | thiazole biosynthetic process |
B | 0000002 | biological_process | mitochondrial genome maintenance |
B | 0005506 | molecular_function | iron ion binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008198 | molecular_function | ferrous iron binding |
B | 0009228 | biological_process | thiamine biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016763 | molecular_function | pentosyltransferase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0052837 | biological_process | thiazole biosynthetic process |
C | 0000002 | biological_process | mitochondrial genome maintenance |
C | 0005506 | molecular_function | iron ion binding |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0008198 | molecular_function | ferrous iron binding |
C | 0009228 | biological_process | thiamine biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0016763 | molecular_function | pentosyltransferase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0052837 | biological_process | thiazole biosynthetic process |
D | 0000002 | biological_process | mitochondrial genome maintenance |
D | 0005506 | molecular_function | iron ion binding |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0008198 | molecular_function | ferrous iron binding |
D | 0009228 | biological_process | thiamine biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0016763 | molecular_function | pentosyltransferase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0052837 | biological_process | thiazole biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 32 |
Details | binding site for residue 48N A 401 |
Chain | Residue |
A | GLY72 |
A | GLY105 |
A | CYS169 |
A | VAL170 |
A | ASP207 |
A | PRO208 |
A | THR234 |
A | THR235 |
A | GLY236 |
A | HIS237 |
A | PHE241 |
A | GLY74 |
A | GLY290 |
A | MET291 |
A | ARG301 |
A | MET302 |
A | GLY303 |
A | THR305 |
A | PHE306 |
A | MET309 |
A | HOH503 |
A | HOH522 |
A | SER75 |
A | HOH527 |
A | HOH530 |
A | HOH532 |
A | SER76 |
A | ILE96 |
A | GLU97 |
A | SER98 |
A | SER99 |
A | GLY104 |
site_id | AC2 |
Number of Residues | 35 |
Details | binding site for residue 48N B 401 |
Chain | Residue |
B | VAL71 |
B | GLY72 |
B | GLY74 |
B | SER75 |
B | SER76 |
B | ILE96 |
B | GLU97 |
B | SER98 |
B | SER99 |
B | GLY104 |
B | GLY105 |
B | CYS169 |
B | VAL170 |
B | ASP207 |
B | PRO208 |
B | THR234 |
B | THR235 |
B | GLY236 |
B | HIS237 |
B | PHE241 |
B | GLY290 |
B | MET291 |
B | ARG301 |
B | MET302 |
B | GLY303 |
B | THR305 |
B | PHE306 |
B | MET309 |
B | HOH502 |
B | HOH509 |
B | HOH524 |
B | HOH525 |
B | HOH532 |
B | HOH541 |
B | HOH573 |
site_id | AC3 |
Number of Residues | 33 |
Details | binding site for residue 48N C 401 |
Chain | Residue |
C | HOH551 |
C | GLY72 |
C | GLY74 |
C | SER75 |
C | SER76 |
C | ILE96 |
C | GLU97 |
C | SER98 |
C | SER99 |
C | GLY104 |
C | GLY105 |
C | CYS169 |
C | VAL170 |
C | ASP207 |
C | PRO208 |
C | THR234 |
C | THR235 |
C | GLY236 |
C | HIS237 |
C | PHE241 |
C | PHE244 |
C | GLY290 |
C | MET291 |
C | ARG301 |
C | MET302 |
C | GLY303 |
C | THR305 |
C | PHE306 |
C | MET309 |
C | HOH501 |
C | HOH519 |
C | HOH522 |
C | HOH532 |
site_id | AC4 |
Number of Residues | 32 |
Details | binding site for residue 48N D 401 |
Chain | Residue |
D | GLY72 |
D | GLY74 |
D | SER75 |
D | SER76 |
D | ILE96 |
D | GLU97 |
D | SER98 |
D | SER99 |
D | GLY104 |
D | GLY105 |
D | CYS169 |
D | VAL170 |
D | ASP207 |
D | PRO208 |
D | THR234 |
D | THR235 |
D | GLY236 |
D | HIS237 |
D | PHE241 |
D | GLY290 |
D | MET291 |
D | ARG301 |
D | MET302 |
D | GLY303 |
D | THR305 |
D | PHE306 |
D | MET309 |
D | HOH501 |
D | HOH525 |
D | HOH527 |
D | HOH539 |
D | HOH567 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 32 |
Details | BINDING: |
Chain | Residue | Details |
A | SER76 | |
B | GLU97 | |
B | GLY105 | |
B | VAL170 | |
B | ASP207 | |
B | HIS237 | |
B | MET291 | |
B | ARG301 | |
C | SER76 | |
C | GLU97 | |
C | GLY105 | |
A | GLU97 | |
C | VAL170 | |
C | ASP207 | |
C | HIS237 | |
C | MET291 | |
C | ARG301 | |
D | SER76 | |
D | GLU97 | |
D | GLY105 | |
D | VAL170 | |
D | ASP207 | |
A | GLY105 | |
D | HIS237 | |
D | MET291 | |
D | ARG301 | |
A | VAL170 | |
A | ASP207 | |
A | HIS237 | |
A | MET291 | |
A | ARG301 | |
B | SER76 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: 2,3-didehydroalanine (Cys) => ECO:0000269|PubMed:22031445 |
Chain | Residue | Details |
A | SER205 | |
B | SER205 | |
C | SER205 | |
D | SER205 |