1NQ5
Glyceraldehyde-3-Phosphate Dehydrogenase Mutant With Cys 149 Replaced By Ser Complexed With Nad+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0005737 | cellular_component | cytoplasm |
| 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 | 0030554 | molecular_function | adenyl nucleotide binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| O | 0000166 | molecular_function | nucleotide binding |
| O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| O | 0005737 | cellular_component | cytoplasm |
| O | 0006006 | biological_process | glucose metabolic process |
| O | 0006096 | biological_process | glycolytic process |
| O | 0016491 | molecular_function | oxidoreductase activity |
| O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| O | 0030554 | molecular_function | adenyl nucleotide binding |
| O | 0050661 | molecular_function | NADP binding |
| O | 0051287 | molecular_function | NAD binding |
| Q | 0000166 | molecular_function | nucleotide binding |
| Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| Q | 0005737 | cellular_component | cytoplasm |
| Q | 0006006 | biological_process | glucose metabolic process |
| Q | 0006096 | biological_process | glycolytic process |
| Q | 0016491 | molecular_function | oxidoreductase activity |
| Q | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| Q | 0030554 | molecular_function | adenyl nucleotide binding |
| Q | 0050661 | molecular_function | NADP binding |
| Q | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 O 1338 |
| Chain | Residue |
| O | THR179 |
| O | ASP181 |
| O | ARG195 |
| O | ARG231 |
| O | NAD1336 |
| O | HOH1407 |
| O | HOH1453 |
| O | HOH1465 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 Q 3338 |
| Chain | Residue |
| Q | ASP181 |
| Q | ARG195 |
| Q | ARG231 |
| Q | HOH1468 |
| Q | NAD3336 |
| Q | THR179 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 5338 |
| Chain | Residue |
| A | THR179 |
| A | ASP181 |
| A | ARG195 |
| A | ARG231 |
| A | HOH1471 |
| A | NAD5336 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 7338 |
| Chain | Residue |
| C | THR179 |
| C | ASP181 |
| C | ARG195 |
| C | ARG231 |
| C | NAD7336 |
| C | HOH7479 |
| site_id | AC5 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD O 1336 |
| Chain | Residue |
| O | GLY7 |
| O | GLY9 |
| O | ARG10 |
| O | ILE11 |
| O | ASN31 |
| O | ASP32 |
| O | GLU76 |
| O | ARG77 |
| O | SER95 |
| O | THR96 |
| O | GLY97 |
| O | PHE99 |
| O | SER119 |
| O | ALA120 |
| O | THR179 |
| O | ASN180 |
| O | ASN313 |
| O | TYR317 |
| O | SO41338 |
| O | HOH1341 |
| O | HOH1356 |
| O | HOH1360 |
| O | HOH1361 |
| O | HOH1382 |
| O | HOH1441 |
| O | HOH1450 |
| O | HOH1453 |
| O | HOH1466 |
| O | HOH1467 |
| Q | LEU187 |
| Q | HOH3426 |
| site_id | AC6 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD Q 3336 |
| Chain | Residue |
| O | LEU187 |
| O | HOH1389 |
| O | HOH1457 |
| Q | GLY7 |
| Q | GLY9 |
| Q | ARG10 |
| Q | ILE11 |
| Q | ASN31 |
| Q | ASP32 |
| Q | LEU33 |
| Q | GLU76 |
| Q | ARG77 |
| Q | SER95 |
| Q | THR96 |
| Q | GLY97 |
| Q | PHE99 |
| Q | SER119 |
| Q | ALA120 |
| Q | ASN180 |
| Q | ASN313 |
| Q | TYR317 |
| Q | HOH1468 |
| Q | SO43338 |
| Q | HOH3342 |
| Q | HOH3374 |
| Q | HOH3385 |
| Q | HOH3419 |
| Q | HOH3482 |
| Q | HOH3499 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 5336 |
| Chain | Residue |
| A | PHE99 |
| A | SER119 |
| A | ALA120 |
| A | THR179 |
| A | ASN180 |
| A | LEU187 |
| A | ASN313 |
| A | HOH1471 |
| A | HOH1473 |
| A | HOH1474 |
| A | SO45338 |
| A | HOH5342 |
| A | HOH5365 |
| A | HOH5366 |
| A | HOH5393 |
| A | HOH5458 |
| A | HOH5468 |
| A | GLY7 |
| A | GLY9 |
| A | ARG10 |
| A | ILE11 |
| A | ASN31 |
| A | ASP32 |
| A | LEU33 |
| A | GLU76 |
| A | ARG77 |
| A | SER95 |
| A | THR96 |
| A | GLY97 |
| A | ARG98 |
| site_id | AC8 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 7336 |
| Chain | Residue |
| C | GLY7 |
| C | GLY9 |
| C | ARG10 |
| C | ILE11 |
| C | ASN31 |
| C | ASP32 |
| C | LEU33 |
| C | ARG77 |
| C | SER95 |
| C | THR96 |
| C | GLY97 |
| C | ARG98 |
| C | SER119 |
| C | ALA120 |
| C | ASN180 |
| C | ASN313 |
| C | TYR317 |
| C | SO47338 |
| C | HOH7342 |
| C | HOH7365 |
| C | HOH7373 |
| C | HOH7374 |
| C | HOH7376 |
| C | HOH7403 |
| C | HOH7411 |
| C | HOH7467 |
| C | HOH7473 |
| C | HOH7479 |
| C | HOH7482 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12569100","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12569100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3586018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9175858","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12569100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3210237","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3586018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9175858","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12569100","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9175858","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18480053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3210237","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3586018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9175858","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"Q6GIL8","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 |
| O | SER149 | |
| O | HIS176 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| Q | SER149 | |
| Q | HIS176 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| A | SER149 | |
| A | HIS176 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| C | SER149 | |
| C | HIS176 |






