4G1K
Crystal structure of triosephosphate isomerase from Burkholderia thailandensis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004807 | molecular_function | triose-phosphate isomerase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016853 | molecular_function | isomerase activity |
A | 0019563 | biological_process | glycerol catabolic process |
A | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
B | 0004807 | molecular_function | triose-phosphate isomerase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016853 | molecular_function | isomerase activity |
B | 0019563 | biological_process | glycerol catabolic process |
B | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
C | 0004807 | molecular_function | triose-phosphate isomerase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006094 | biological_process | gluconeogenesis |
C | 0006096 | biological_process | glycolytic process |
C | 0016853 | molecular_function | isomerase activity |
C | 0019563 | biological_process | glycerol catabolic process |
C | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
D | 0004807 | molecular_function | triose-phosphate isomerase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006094 | biological_process | gluconeogenesis |
D | 0006096 | biological_process | glycolytic process |
D | 0016853 | molecular_function | isomerase activity |
D | 0019563 | biological_process | glycerol catabolic process |
D | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 301 |
Chain | Residue |
A | PHE223 |
A | GLN225 |
A | ILE228 |
A | HOH543 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | GLY124 |
A | LEU125 |
A | ARG165 |
A | HOH485 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | GLY21 |
A | ASN22 |
A | HOH497 |
A | HOH530 |
A | GLY17 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 304 |
Chain | Residue |
A | ARG118 |
A | LEU121 |
A | ALA122 |
A | GLU162 |
A | ARG165 |
D | ARG165 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 301 |
Chain | Residue |
B | PHE223 |
B | GLN225 |
B | ILE228 |
B | HOH513 |
B | HOH554 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | GLY124 |
B | LEU125 |
B | ARG165 |
B | HOH434 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
B | GLY17 |
B | GLY21 |
B | ASN22 |
B | LEU25 |
B | HOH525 |
B | HOH526 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 304 |
Chain | Residue |
B | ARG8 |
B | TYR94 |
B | THR126 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA C 301 |
Chain | Residue |
C | PHE223 |
C | GLN225 |
C | ILE228 |
C | HOH462 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 302 |
Chain | Residue |
B | GLY124 |
C | GLY124 |
C | LEU125 |
C | THR126 |
C | ARG165 |
C | HOH437 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 303 |
Chain | Residue |
C | GLY17 |
C | GLY21 |
C | ASN22 |
C | LEU25 |
C | LEU238 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 304 |
Chain | Residue |
C | ARG8 |
C | SER64 |
C | THR126 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA D 301 |
Chain | Residue |
D | PHE223 |
D | GLN225 |
D | ILE228 |
D | HOH475 |
D | HOH506 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 302 |
Chain | Residue |
D | GLY124 |
D | LEU125 |
D | THR126 |
D | ARG165 |
D | HOH417 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT D 303 |
Chain | Residue |
D | SER213 |
D | GLY234 |
D | GLY235 |
D | HOH407 |
D | HOH477 |
D | HOH500 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 304 |
Chain | Residue |
D | HIS16 |
D | GLY21 |
D | ASN22 |
D | LEU25 |
D | LEU238 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 26 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGTGKSATAEqAqqvhaflrgr........LAAK |
Chain | Residue | Details |
A | ILE176-LYS201 |
site_id | PS00171 |
Number of Residues | 11 |
Details | TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG |
Chain | Residue | Details |
A | ALA169-GLY179 |