1DSS
STRUCTURE OF ACTIVE-SITE CARBOXYMETHYLATED D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM PALINURUS VERSICOLOR
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 | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 G 501 |
| Chain | Residue |
| G | GLY209 |
| G | HOH584 |
| G | HOH620 |
| G | HOH678 |
| G | HOH717 |
| G | SER148 |
| G | CCS149 |
| G | THR150 |
| G | HIS176 |
| G | THR208 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 G 502 |
| Chain | Residue |
| G | CCS149 |
| G | THR179 |
| G | THR181 |
| G | ARG231 |
| G | NAD335 |
| G | HOH530 |
| G | HOH717 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 R 501 |
| Chain | Residue |
| R | SER148 |
| R | CCS149 |
| R | THR150 |
| R | HIS176 |
| R | THR208 |
| R | GLY209 |
| R | HOH611 |
| R | HOH675 |
| R | HOH676 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 R 502 |
| Chain | Residue |
| R | CCS149 |
| R | THR179 |
| R | THR181 |
| R | ARG231 |
| R | NAD335 |
| R | HOH585 |
| R | HOH675 |
| site_id | AC5 |
| Number of Residues | 35 |
| 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 | CCS149 |
| G | ALA180 |
| G | ASN313 |
| G | GLU314 |
| G | TYR317 |
| G | SO4502 |
| G | HOH505 |
| G | HOH506 |
| G | HOH512 |
| G | HOH513 |
| G | HOH530 |
| G | HOH535 |
| G | HOH536 |
| G | HOH544 |
| G | HOH552 |
| G | HOH598 |
| G | HOH619 |
| G | HOH622 |
| G | HOH651 |
| site_id | AC6 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NAD R 335 |
| Chain | Residue |
| R | HOH534 |
| R | HOH535 |
| R | HOH544 |
| R | HOH585 |
| R | HOH589 |
| R | HOH590 |
| R | HOH591 |
| R | HOH615 |
| R | HOH656 |
| R | ASN6 |
| R | GLY7 |
| R | GLY9 |
| R | ARG10 |
| R | ILE11 |
| R | ASN31 |
| R | ASP32 |
| R | PRO33 |
| R | PHE34 |
| R | GLU76 |
| R | MET77 |
| R | SER95 |
| R | THR96 |
| R | GLY97 |
| R | PHE99 |
| R | SER119 |
| R | ALA120 |
| R | CCS149 |
| R | ALA180 |
| R | ASN313 |
| R | GLU314 |
| R | TYR317 |
| R | SO4502 |
| R | HOH510 |
| R | HOH511 |
| R | HOH512 |
| R | HOH533 |
| site_id | AVG |
| Number of Residues | 2 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| G | CCS149 |
| G | HIS176 |
| site_id | AVR |
| Number of Residues | 2 |
| Details | ACTIVE SITE. |
| Chain | Residue |
| R | CCS149 |
| R | 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 | 8 |
| 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 | 1 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| G | HIS176 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| 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 |
