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STRUCTURE OF HOLO-GLYCERALDEHYDE-3-PHOSPHATE-DEHYDROGENASE FROM PALINURUS VERSICOLOR REFINED 2.0 ANGSTROM RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| G | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0006006 | biological_process | glucose metabolic process |
| G | 0006096 | biological_process | glycolytic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| G | 0050661 | molecular_function | NADP binding |
| G | 0051287 | molecular_function | NAD binding |
| R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| R | 0005737 | cellular_component | cytoplasm |
| R | 0005829 | cellular_component | cytosol |
| R | 0006006 | biological_process | glucose metabolic process |
| R | 0006096 | biological_process | glycolytic process |
| R | 0016491 | molecular_function | oxidoreductase activity |
| R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| R | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| R | 0050661 | molecular_function | NADP binding |
| R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 G 501 |
| Chain | Residue |
| G | SER148 |
| G | THR208 |
| G | GLY209 |
| G | ALA210 |
| G | HOH541 |
| G | HOH600 |
| G | HOH671 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 G 502 |
| Chain | Residue |
| G | THR179 |
| G | THR181 |
| G | ARG231 |
| G | NAD335 |
| G | HOH546 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 R 501 |
| Chain | Residue |
| R | SER148 |
| R | THR208 |
| R | GLY209 |
| R | ALA210 |
| R | HOH616 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 R 502 |
| Chain | Residue |
| R | THR179 |
| R | THR181 |
| R | ARG231 |
| R | NAD335 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD G 335 |
| Chain | Residue |
| G | ASN6 |
| G | GLY7 |
| G | PHE8 |
| G | GLY9 |
| G | ARG10 |
| G | ILE11 |
| G | ASN31 |
| G | ASP32 |
| G | PRO33 |
| G | PHE34 |
| G | MET77 |
| G | SER95 |
| G | THR96 |
| G | GLY97 |
| G | SER119 |
| G | ALA120 |
| G | CYS149 |
| G | ALA180 |
| G | ASN313 |
| G | TYR317 |
| G | SO4502 |
| G | HOH505 |
| G | HOH513 |
| G | HOH514 |
| G | HOH522 |
| G | HOH577 |
| G | HOH601 |
| G | HOH619 |
| G | HOH636 |
| G | HOH688 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD R 335 |
| Chain | Residue |
| R | ASN6 |
| R | GLY7 |
| R | GLY9 |
| R | ARG10 |
| R | ILE11 |
| R | ASN31 |
| R | ASP32 |
| R | PRO33 |
| R | PHE34 |
| R | MET77 |
| R | SER95 |
| R | THR96 |
| R | GLY97 |
| R | SER119 |
| R | ALA120 |
| R | CYS149 |
| R | ASN313 |
| R | SO4502 |
| R | HOH507 |
| R | HOH508 |
| R | HOH522 |
| R | HOH595 |
| R | HOH596 |
| R | HOH597 |
| site_id | ACT |
| Number of Residues | 2 |
| Details | ACTIVE SITE RESIDUES CYS 149 AND HIS 176 |
| Chain | Residue |
| G | CYS149 |
| G | HIS176 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| G | ALA147-LEU154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9761850","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Activates thiol group during catalysis"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| 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 | a catalytic site defined by CSA, PubMed 9144771 |
| Chain | Residue | Details |
| G | CYS149 | |
| G | HIS176 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 9144771 |
| Chain | Residue | Details |
| R | CYS149 | |
| R | HIS176 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 911 |
| Chain | Residue | Details |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 911 |
| Chain | Residue | Details |
