1B7G
GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE
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 | 0006096 | biological_process | glycolytic process |
O | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
O | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
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 | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity |
O | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
O | 0050661 | molecular_function | NADP binding |
O | 0051287 | molecular_function | NAD binding |
Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
Q | 0005737 | cellular_component | cytoplasm |
Q | 0006096 | biological_process | glycolytic process |
Q | 0008839 | molecular_function | 4-hydroxy-tetrahydrodipicolinate reductase |
Q | 0009089 | biological_process | lysine biosynthetic process via diaminopimelate |
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 | 0043891 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity |
Q | 0047100 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity |
Q | 0050661 | molecular_function | NADP binding |
Q | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 O 601 |
Chain | Residue |
O | SER138 |
O | CYS139 |
O | ASN140 |
O | ARG166 |
O | HIS192 |
O | HIS193 |
O | HOH617 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 Q 602 |
Chain | Residue |
Q | SER138 |
Q | CYS139 |
Q | ASN140 |
Q | ARG166 |
Q | HIS192 |
Q | HIS193 |
Q | HOH667 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 O 603 |
Chain | Residue |
O | ARG166 |
O | ARG167 |
O | HOH661 |
O | HOH847 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 Q 604 |
Chain | Residue |
Q | ARG166 |
Q | ARG167 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 O 605 |
Chain | Residue |
O | LYS33 |
O | THR34 |
O | SER35 |
O | HOH777 |
O | HOH894 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 Q 606 |
Chain | Residue |
Q | LYS33 |
Q | THR34 |
Q | SER35 |
Q | HOH744 |
Q | HOH745 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 O 607 |
Chain | Residue |
O | PRO186 |
O | SER191 |
O | HIS192 |
O | HOH636 |
O | HOH728 |
O | HOH784 |
O | HOH799 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 Q 608 |
Chain | Residue |
Q | PRO186 |
Q | SER191 |
Q | HIS192 |
Q | HOH736 |
Q | HOH792 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 Q 609 |
Chain | Residue |
O | LYS131 |
Q | ARG49 |
Q | PRO66 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 O 610 |
Chain | Residue |
O | THR11 |
O | LYS172 |
O | GLU173 |
O | HOH664 |
O | HOH688 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 O 611 |
Chain | Residue |
O | LYS111 |
O | ALA112 |
O | LYS195 |
O | HOH645 |
O | HOH675 |
O | HOH762 |
O | HOH839 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 Q 612 |
Chain | Residue |
Q | GLY10 |
Q | THR11 |
Q | LYS172 |
Q | HOH640 |
site_id | CTO |
Number of Residues | 2 |
Details | CATALYTIC SITE IN SUBUNIT O |
Chain | Residue |
O | CYS139 |
O | HIS219 |
site_id | CTQ |
Number of Residues | 2 |
Details | CATALYTIC SITE IN SUBUNIT Q |
Chain | Residue |
Q | CYS139 |
Q | HIS219 |
site_id | PIO |
Number of Residues | 5 |
Details | INORGANIC PHOSPHATE BINDING SITE IN SUBUNIT Q |
Chain | Residue |
O | SER138 |
O | ASN140 |
O | ARG166 |
O | HIS192 |
O | HIS193 |
site_id | PIQ |
Number of Residues | 5 |
Details | INORGAINC PHOSPHATE BINDING SITE IN SUBUNIT Q |
Chain | Residue |
Q | SER138 |
Q | ASN140 |
Q | ARG166 |
Q | HIS192 |
Q | HIS193 |
site_id | PSO |
Number of Residues | 2 |
Details | SUBSTRATE PHOSPHARE BINDING SITE IN SUBUNIT O |
Chain | Residue |
O | ARG166 |
O | ARG167 |
site_id | PSQ |
Number of Residues | 2 |
Details | SUBSTRATE PHOSPHATE BINDING SITE IN SUBUNIT Q |
Chain | Residue |
Q | ARG166 |
Q | ARG167 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. VSCNTTaL |
Chain | Residue | Details |
O | VAL137-LEU144 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
O | CYS139 | |
Q | CYS139 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
O | THR11 | |
Q | ARG167 | |
Q | HIS193 | |
Q | GLN300 | |
O | GLY109 | |
O | SER138 | |
O | ARG167 | |
O | HIS193 | |
O | GLN300 | |
Q | THR11 | |
Q | GLY109 | |
Q | SER138 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
O | CYS139 | |
O | HIS219 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
Q | CYS139 | |
Q | HIS219 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
O | ARG166 | |
O | CYS139 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
Q | ARG166 | |
Q | CYS139 |