1IHX
Crystal structure of two D-glyceraldehyde-3-phosphate dehydrogenase complexes: a case of asymmetry
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0005737 | cellular_component | cytoplasm |
| 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 | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| D | 0005737 | cellular_component | cytoplasm |
| 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 | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | SER148 |
| A | THR208 |
| A | GLY209 |
| A | ALA210 |
| A | HOH562 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 502 |
| Chain | Residue |
| B | ALA210 |
| B | HOH563 |
| B | SER148 |
| B | THR150 |
| B | THR208 |
| B | GLY209 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 503 |
| Chain | Residue |
| C | SER148 |
| C | THR208 |
| C | GLY209 |
| C | ALA210 |
| C | HOH555 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 504 |
| Chain | Residue |
| D | SER148 |
| D | THR150 |
| D | THR208 |
| D | GLY209 |
| D | ALA210 |
| D | HOH552 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | THR179 |
| A | THR181 |
| A | ARG231 |
| A | SND335 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 506 |
| Chain | Residue |
| B | THR179 |
| B | THR181 |
| B | ARG231 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 507 |
| Chain | Residue |
| C | THR179 |
| C | THR181 |
| C | ARG231 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 508 |
| Chain | Residue |
| D | THR179 |
| D | THR181 |
| D | ARG231 |
| D | SND338 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE SND A 335 |
| Chain | Residue |
| A | ASN6 |
| A | GLY7 |
| A | PHE8 |
| A | GLY9 |
| A | ARG10 |
| A | ILE11 |
| A | ASP32 |
| A | PRO33 |
| A | PHE34 |
| A | ILE35 |
| A | MET77 |
| A | SER95 |
| A | THR96 |
| A | SER119 |
| A | ALA120 |
| A | SO4505 |
| A | HOH506 |
| A | HOH559 |
| A | HOH560 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SND B 336 |
| Chain | Residue |
| B | ASN6 |
| B | GLY7 |
| B | PHE8 |
| B | GLY9 |
| B | ARG10 |
| B | ILE11 |
| B | ASN31 |
| B | ASP32 |
| B | PRO33 |
| B | PHE34 |
| B | ILE35 |
| B | MET77 |
| B | THR96 |
| B | GLY97 |
| B | PHE99 |
| B | SER119 |
| B | ALA120 |
| B | HOH509 |
| B | HOH531 |
| B | HOH572 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SND C 337 |
| Chain | Residue |
| C | ASN6 |
| C | GLY7 |
| C | GLY9 |
| C | ARG10 |
| C | ILE11 |
| C | ASN31 |
| C | ASP32 |
| C | PRO33 |
| C | PHE34 |
| C | ILE35 |
| C | MET77 |
| C | SER95 |
| C | THR96 |
| C | GLY97 |
| C | PHE99 |
| C | SER119 |
| C | CYS149 |
| C | ASN313 |
| C | TYR317 |
| C | HOH547 |
| site_id | BC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE SND D 338 |
| Chain | Residue |
| D | ARG10 |
| D | ILE11 |
| D | ASN31 |
| D | ASP32 |
| D | PRO33 |
| D | PHE34 |
| D | MET77 |
| D | THR96 |
| D | GLY97 |
| D | PHE99 |
| D | SER119 |
| D | ALA120 |
| D | CYS149 |
| D | ASN313 |
| D | SO4508 |
| D | HOH511 |
| D | HOH515 |
| D | HOH538 |
| D | HOH542 |
| B | HOH555 |
| D | ASN6 |
| D | PHE8 |
| D | GLY9 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| A | ALA147-LEU154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9761850","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Activates thiol group during catalysis"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"P00357","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| A | CYS149 | |
| A | HIS176 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| B | CYS149 | |
| B | HIS176 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| C | CYS149 | |
| C | HIS176 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| D | CYS149 | |
| D | HIS176 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 911 |
| Chain | Residue | Details |
| A | CYS149 | covalent catalysis, proton shuttle (general acid/base) |
| A | HIS176 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 911 |
| Chain | Residue | Details |
| B | CYS149 | covalent catalysis, proton shuttle (general acid/base) |
| B | HIS176 | proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 2 |
| Details | M-CSA 911 |
| Chain | Residue | Details |
| C | CYS149 | covalent catalysis, proton shuttle (general acid/base) |
| C | HIS176 | proton shuttle (general acid/base) |
| site_id | MCSA4 |
| Number of Residues | 2 |
| Details | M-CSA 911 |
| Chain | Residue | Details |
| D | CYS149 | covalent catalysis, proton shuttle (general acid/base) |
| D | HIS176 | proton shuttle (general acid/base) |
