3E5R
Crystal structure and Functional Analysis of Glyceraldehyde-3-phosphate Dehydrogenase from Oryza Sativa
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 | 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 | 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 | 0050661 | molecular_function | NADP binding |
C | 0051287 | molecular_function | NAD binding |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
O | 0005737 | cellular_component | cytoplasm |
O | 0005829 | cellular_component | cytosol |
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 | 0050661 | molecular_function | NADP binding |
O | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAD O 5463 |
Chain | Residue |
B | PRO193 |
O | PRO36 |
O | THR101 |
O | GLY102 |
O | SER124 |
O | ALA125 |
O | CYS154 |
O | ALA185 |
O | ASN318 |
O | GLU319 |
O | HOH5493 |
O | ASN9 |
O | HOH5521 |
O | HOH5559 |
O | GLY10 |
O | PHE11 |
O | GLY12 |
O | ARG13 |
O | ILE14 |
O | ASN34 |
O | ASP35 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD A 5466 |
Chain | Residue |
A | ASN9 |
A | GLY10 |
A | PHE11 |
A | GLY12 |
A | ARG13 |
A | ILE14 |
A | ASN34 |
A | ASP35 |
A | PRO36 |
A | PHE37 |
A | ARG82 |
A | THR101 |
A | GLY102 |
A | PHE104 |
A | SER124 |
A | ALA125 |
A | PRO126 |
A | CYS154 |
A | ALA185 |
A | ASN318 |
A | TYR322 |
A | HOH5626 |
A | HOH5684 |
C | PRO193 |
C | HOH5801 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD B 5465 |
Chain | Residue |
B | ASN9 |
B | GLY10 |
B | PHE11 |
B | GLY12 |
B | ARG13 |
B | ILE14 |
B | ASN34 |
B | ASP35 |
B | PRO36 |
B | PHE37 |
B | ILE38 |
B | ARG82 |
B | THR101 |
B | GLY102 |
B | PHE104 |
B | SER124 |
B | ALA125 |
B | CYS154 |
B | ALA185 |
B | ASN318 |
B | GLU319 |
B | TYR322 |
B | HOH5485 |
B | HOH5527 |
B | HOH5562 |
B | HOH5573 |
B | HOH5657 |
O | HOH5551 |
site_id | AC4 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD C 5467 |
Chain | Residue |
C | HOH5797 |
A | PRO193 |
A | HOH5768 |
C | ASN9 |
C | GLY10 |
C | PHE11 |
C | GLY12 |
C | ARG13 |
C | ILE14 |
C | ASN34 |
C | ASP35 |
C | PRO36 |
C | PHE37 |
C | ILE38 |
C | ARG82 |
C | THR101 |
C | GLY102 |
C | SER124 |
C | ALA125 |
C | CYS154 |
C | ALA185 |
C | ASN318 |
C | GLU319 |
C | TYR322 |
C | HOH5607 |
C | HOH5614 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
O | ALA152-LEU159 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10009 |
Chain | Residue | Details |
O | CYS154 | |
A | CYS154 | |
B | CYS154 | |
C | CYS154 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22903596 |
Chain | Residue | Details |
O | ARG13 | |
C | ARG13 | |
C | ASP35 | |
C | ARG82 | |
O | ASP35 | |
O | ARG82 | |
A | ARG13 | |
A | ASP35 | |
A | ARG82 | |
B | ARG13 | |
B | ASP35 | |
B | ARG82 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
O | SER153 | |
A | ASN318 | |
B | SER153 | |
B | THR184 | |
B | THR213 | |
B | ARG236 | |
B | ASN318 | |
C | SER153 | |
C | THR184 | |
C | THR213 | |
C | ARG236 | |
O | THR184 | |
C | ASN318 | |
O | THR213 | |
O | ARG236 | |
O | ASN318 | |
A | SER153 | |
A | THR184 | |
A | THR213 | |
A | ARG236 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000250 |
Chain | Residue | Details |
O | HIS181 | |
A | HIS181 | |
B | HIS181 | |
C | HIS181 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
O | HIS181 | |
O | CYS154 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
A | HIS181 | |
A | CYS154 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
B | HIS181 | |
B | CYS154 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
C | HIS181 | |
C | CYS154 |