2B4R
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 Angstrom Resolution reveals intriguing extra electron density in the active site
Replaces: 1ZYAFunctional Information from GO Data
Chain | GOid | namespace | contents |
O | 0000166 | molecular_function | nucleotide binding |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
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 |
P | 0000166 | molecular_function | nucleotide binding |
P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
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 | 0050661 | molecular_function | NADP binding |
P | 0051287 | molecular_function | NAD binding |
Q | 0000166 | molecular_function | nucleotide binding |
Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
Q | 0005829 | cellular_component | cytosol |
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 | 0050661 | molecular_function | NADP binding |
Q | 0051287 | molecular_function | NAD binding |
R | 0000166 | molecular_function | nucleotide binding |
R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
R | 0005829 | cellular_component | cytosol |
R | 0006006 | biological_process | glucose metabolic process |
R | 0006096 | biological_process | glycolytic process |
R | 0016491 | molecular_function | oxidoreductase activity |
R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
R | 0050661 | molecular_function | NADP binding |
R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD Q 501 |
Chain | Residue |
P | HOH767 |
Q | SER98 |
Q | THR99 |
Q | GLY100 |
Q | PHE102 |
Q | SER122 |
Q | ALA123 |
Q | CYS153 |
Q | THR183 |
Q | ALA184 |
Q | ASN319 |
Q | GLY10 |
Q | TYR323 |
Q | HOH513 |
Q | HOH522 |
Q | HOH523 |
Q | HOH549 |
Q | HOH550 |
Q | PHE11 |
Q | GLY12 |
Q | ARG13 |
Q | ILE14 |
Q | ASP35 |
Q | PRO36 |
Q | PHE37 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD P 701 |
Chain | Residue |
P | ASN9 |
P | GLY10 |
P | GLY12 |
P | ARG13 |
P | ILE14 |
P | ASN34 |
P | ASP35 |
P | PRO36 |
P | PHE37 |
P | LYS80 |
P | SER98 |
P | THR99 |
P | GLY100 |
P | SER122 |
P | ALA123 |
P | CYS153 |
P | ALA184 |
P | ASN319 |
P | TYR323 |
P | AES602 |
P | HOH707 |
P | HOH711 |
P | HOH720 |
P | HOH727 |
P | HOH732 |
P | HOH740 |
P | HOH754 |
site_id | AC3 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD O 801 |
Chain | Residue |
O | ASN9 |
O | GLY10 |
O | PHE11 |
O | GLY12 |
O | ARG13 |
O | ILE14 |
O | ASN34 |
O | ASP35 |
O | PRO36 |
O | PHE37 |
O | MET38 |
O | GLU79 |
O | LYS80 |
O | SER98 |
O | THR99 |
O | GLY100 |
O | SER122 |
O | ALA123 |
O | CYS153 |
O | ALA184 |
O | ASN319 |
O | TYR323 |
O | AES601 |
O | HOH812 |
O | HOH829 |
O | HOH842 |
O | HOH847 |
O | HOH853 |
R | HOH963 |
site_id | AC4 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD R 901 |
Chain | Residue |
R | ASN319 |
R | TYR323 |
R | AES603 |
R | HOH904 |
R | HOH907 |
R | HOH910 |
R | HOH918 |
R | HOH923 |
R | HOH939 |
R | HOH941 |
R | HOH942 |
R | ASN9 |
R | GLY10 |
R | GLY12 |
R | ARG13 |
R | ILE14 |
R | ASN34 |
R | ASP35 |
R | PRO36 |
R | PHE37 |
R | GLU79 |
R | LYS80 |
R | SER98 |
R | THR99 |
R | GLY100 |
R | PHE102 |
R | SER122 |
R | ALA123 |
R | ALA184 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE AES O 601 |
Chain | Residue |
O | THR183 |
O | ASN185 |
O | NAD801 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE AES P 602 |
Chain | Residue |
P | THR183 |
P | ASN185 |
P | ARG237 |
P | NAD701 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE AES R 603 |
Chain | Residue |
R | THR183 |
R | ASN185 |
R | NAD901 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL R 503 |
Chain | Residue |
Q | GLY196 |
Q | LYS197 |
Q | ASP198 |
Q | TRP199 |
R | GLU283 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL P 703 |
Chain | Residue |
O | GLU283 |
P | GLY196 |
P | ASP198 |
P | TRP199 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL O 804 |
Chain | Residue |
O | ASP292 |
O | ASN293 |
O | ARG294 |
R | GLU71 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL R 903 |
Chain | Residue |
Q | GLU283 |
R | ASP198 |
R | TRP199 |
Functional Information from PROSITE/UniProt
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
O | HIS180 | |
O | CYS153 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
P | HIS180 | |
P | CYS153 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
Q | HIS180 | |
Q | CYS153 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
R | HIS180 | |
R | CYS153 |