3IDS
Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi in complex with the irreversible iodoacetamide inhibitor
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
A | 0005829 | cellular_component | cytosol |
A | 0006006 | biological_process | glucose metabolic process |
A | 0006096 | biological_process | glycolytic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0020015 | cellular_component | glycosome |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
B | 0005829 | cellular_component | cytosol |
B | 0006006 | biological_process | glucose metabolic process |
B | 0006096 | biological_process | glycolytic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0020015 | cellular_component | glycosome |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
C | 0005829 | cellular_component | cytosol |
C | 0006006 | biological_process | glucose metabolic process |
C | 0006096 | biological_process | glycolytic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
C | 0020015 | cellular_component | glycosome |
C | 0050661 | molecular_function | NADP binding |
C | 0051287 | molecular_function | NAD binding |
D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
D | 0005829 | cellular_component | cytosol |
D | 0006006 | biological_process | glucose metabolic process |
D | 0006096 | biological_process | glycolytic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0020015 | cellular_component | glycosome |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACM C 360 |
Chain | Residue |
C | SER165 |
C | CYS166 |
C | ASN335 |
C | TYR339 |
C | HOH545 |
C | HOH716 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL C 361 |
Chain | Residue |
C | HOH389 |
C | HOH412 |
C | HOH533 |
C | LEU296 |
C | ASP300 |
C | ASP304 |
site_id | AC3 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD D 360 |
Chain | Residue |
D | GLY9 |
D | GLY11 |
D | ARG12 |
D | ILE13 |
D | VAL37 |
D | ASP38 |
D | MET39 |
D | ALA90 |
D | GLN91 |
D | SER110 |
D | THR111 |
D | GLY112 |
D | LEU113 |
D | SER134 |
D | ALA135 |
D | CYS166 |
D | ALA198 |
D | ASN335 |
D | TYR339 |
D | HOH384 |
D | HOH394 |
D | HOH395 |
D | HOH412 |
D | HOH436 |
D | HOH569 |
D | HOH860 |
D | HOH883 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 361 |
Chain | Residue |
D | TYR291 |
D | THR292 |
D | ASP293 |
D | HOH397 |
D | HOH490 |
D | HOH1084 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL D 362 |
Chain | Residue |
D | VAL104 |
D | GLY127 |
D | ARG129 |
D | HOH663 |
D | HOH1164 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACM A 360 |
Chain | Residue |
A | CYS166 |
A | ASN335 |
A | HOH432 |
A | HOH511 |
A | HOH512 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 361 |
Chain | Residue |
A | ASP300 |
A | ASP304 |
A | HOH459 |
A | HOH462 |
A | HOH499 |
C | LYS58 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 362 |
Chain | Residue |
A | ASP24 |
A | GLY25 |
A | GLU30 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACM B 360 |
Chain | Residue |
B | SER165 |
B | CYS166 |
B | ASN335 |
B | HOH706 |
B | HOH873 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 361 |
Chain | Residue |
B | TYR291 |
B | THR292 |
B | ASP293 |
B | HOH424 |
B | HOH467 |
B | HOH587 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
C | ALA164-LEU171 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
C | CYS166 | |
D | CYS166 | |
A | CYS166 | |
B | CYS166 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12795610, ECO:0000269|PubMed:14622286 |
Chain | Residue | Details |
C | ARG12 | |
D | ASN335 | |
A | ARG12 | |
A | ASP38 | |
A | GLN91 | |
A | SER134 | |
A | ASN335 | |
B | ARG12 | |
B | ASP38 | |
B | GLN91 | |
B | SER134 | |
C | ASP38 | |
B | ASN335 | |
C | GLN91 | |
C | SER134 | |
C | ASN335 | |
D | ARG12 | |
D | ASP38 | |
D | GLN91 | |
D | SER134 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
C | SER165 | |
A | THR197 | |
A | THR226 | |
A | ARG249 | |
B | SER165 | |
B | THR197 | |
B | THR226 | |
B | ARG249 | |
C | THR197 | |
C | THR226 | |
C | ARG249 | |
D | SER165 | |
D | THR197 | |
D | THR226 | |
D | ARG249 | |
A | SER165 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis |
Chain | Residue | Details |
C | HIS194 | |
D | HIS194 | |
A | HIS194 | |
B | HIS194 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
C | CYS166 | |
C | HIS194 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
D | CYS166 | |
D | HIS194 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
A | CYS166 | |
A | HIS194 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
B | CYS166 | |
B | HIS194 |