2I5P
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase isoform 1 from K. marxianus
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0030312 | cellular_component | external encapsulating structure |
O | 0050661 | molecular_function | NADP binding |
O | 0051287 | molecular_function | NAD binding |
P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
P | 0005737 | cellular_component | cytoplasm |
P | 0005829 | cellular_component | cytosol |
P | 0006006 | biological_process | glucose metabolic process |
P | 0006096 | biological_process | glycolytic process |
P | 0016491 | molecular_function | oxidoreductase activity |
P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
P | 0030312 | cellular_component | external encapsulating structure |
P | 0050661 | molecular_function | NADP binding |
P | 0051287 | molecular_function | NAD binding |
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 | ALA147-LEU154 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P22513, ECO:0000255|PROSITE-ProRule:PRU10009 |
Chain | Residue | Details |
O | CYS149 | |
P | CYS649 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P22513 |
Chain | Residue | Details |
O | GLU76 | |
O | SER148 | |
O | THR179 | |
O | THR208 | |
O | ARG231 | |
O | ASN313 | |
P | ARG510 | |
P | ASP532 | |
P | GLU576 | |
P | SER648 | |
P | THR679 | |
P | THR708 | |
P | ARG731 | |
P | ASN813 | |
O | ARG10 | |
O | ASP32 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P22513 |
Chain | Residue | Details |
O | HIS176 | |
P | HIS676 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00359 |
Chain | Residue | Details |
O | SER200 | |
P | SER648 | |
P | SER677 | |
P | SER700 | |
O | SER148 | |
O | SER177 |