2I9E
Structure of Triosephosphate Isomerase of Tenebrio molitor
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004807 | molecular_function | triose-phosphate isomerase activity |
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 | 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 | 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 | 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 | 5 |
Details | BINDING SITE FOR RESIDUE TRS C 1001 |
Chain | Residue |
C | PHE101 |
C | GLY102 |
D | PHE101 |
D | GLY102 |
D | TRS1003 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TRS B 1002 |
Chain | Residue |
B | GLY102 |
B | HOH1074 |
A | PHE101 |
A | GLY102 |
B | ILE100 |
B | PHE101 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS D 1003 |
Chain | Residue |
C | ILE100 |
C | PHE101 |
C | TRS1001 |
D | PHE101 |
D | GLY102 |
D | GLU103 |
D | LEU107 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TRS B 1004 |
Chain | Residue |
B | ASN10 |
B | TRP11 |
B | LYS12 |
B | ASN14 |
B | GLY231 |
B | GLY232 |
B | LEU235 |
B | HOH1088 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TRS D 1005 |
Chain | Residue |
C | GLY71 |
D | ASN14 |
D | GLU117 |
D | LEU235 |
Functional Information from PROSITE/UniProt
site_id | PS00171 |
Number of Residues | 11 |
Details | TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG |
Chain | Residue | Details |
A | ALA162-GLY172 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1hti |
Chain | Residue | Details |
A | ASN10 | |
A | GLU164 | |
A | GLY170 | |
A | HIS94 | |
A | LYS12 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1hti |
Chain | Residue | Details |
B | ASN10 | |
B | GLU164 | |
B | GLY170 | |
B | HIS94 | |
B | LYS12 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1hti |
Chain | Residue | Details |
C | ASN10 | |
C | GLU164 | |
C | GLY170 | |
C | HIS94 | |
C | LYS12 |
site_id | CSA4 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1hti |
Chain | Residue | Details |
D | ASN10 | |
D | GLU164 | |
D | GLY170 | |
D | HIS94 | |
D | LYS12 |