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 | ACT_SITE: Nucleophile => ECO:0000269|PubMed:18480053, ECO:0000305|PubMed:12569100 |
Chain | Residue | Details |
O | THR150 | |
Q | THR150 | |
A | THR150 | |
C | THR150 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 |
Chain | Residue | Details |
O | ILE11 | |
Q | ALA120 | |
Q | ASP181 | |
Q | GLU314 | |
A | ILE11 | |
A | LEU33 | |
A | ASP78 | |
A | ALA120 | |
A | ASP181 | |
A | GLU314 | |
C | ILE11 | |
O | LEU33 | |
C | LEU33 | |
C | ASP78 | |
C | ALA120 | |
C | ASP181 | |
C | GLU314 | |
O | ASP78 | |
O | ALA120 | |
O | ASP181 | |
O | GLU314 | |
Q | ILE11 | |
Q | LEU33 | |
Q | ASP78 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 |
Chain | Residue | Details |
O | SER149 | |
C | SER149 | |
C | ASN180 | |
C | VAL232 | |
O | ASN180 | |
O | VAL232 | |
Q | SER149 | |
Q | ASN180 | |
Q | VAL232 | |
A | SER149 | |
A | ASN180 | |
A | VAL232 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12569100, ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:9175858 |
Chain | Residue | Details |
O | ALA196 | |
Q | ALA196 | |
A | ALA196 | |
C | ALA196 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18480053, ECO:0000269|PubMed:3210237, ECO:0000269|PubMed:3586018, ECO:0000269|PubMed:9175858 |
Chain | Residue | Details |
O | GLY209 | |
Q | GLY209 | |
A | GLY209 | |
C | GLY209 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:Q6GIL8 |
Chain | Residue | Details |
O | SER177 | |
Q | SER177 | |
A | SER177 | |
C | SER177 |
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 |