3GNQ
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase, type I from Burkholderia pseudomallei
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0006006 | biological_process | glucose metabolic 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 | 0000166 | molecular_function | nucleotide binding |
B | 0006006 | biological_process | glucose metabolic 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 | 0000166 | molecular_function | nucleotide binding |
C | 0006006 | biological_process | glucose metabolic 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 |
D | 0000166 | molecular_function | nucleotide binding |
D | 0006006 | biological_process | glucose metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0006006 | biological_process | glucose metabolic process |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
E | 0050661 | molecular_function | NADP binding |
E | 0051287 | molecular_function | NAD binding |
F | 0000166 | molecular_function | nucleotide binding |
F | 0006006 | biological_process | glucose metabolic process |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
F | 0050661 | molecular_function | NADP binding |
F | 0051287 | molecular_function | NAD binding |
G | 0000166 | molecular_function | nucleotide binding |
G | 0006006 | biological_process | glucose metabolic process |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
G | 0050661 | molecular_function | NADP binding |
G | 0051287 | molecular_function | NAD binding |
H | 0000166 | molecular_function | nucleotide binding |
H | 0006006 | biological_process | glucose metabolic process |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
H | 0050661 | molecular_function | NADP binding |
H | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD B 901 |
Chain | Residue |
B | GLY8 |
B | THR99 |
B | GLY100 |
B | PHE101 |
B | SER122 |
B | ALA123 |
B | CYS154 |
B | ASN185 |
B | ASN316 |
B | PHE320 |
B | HOH348 |
B | GLY10 |
B | HOH350 |
B | HOH360 |
B | HOH381 |
B | HOH517 |
B | HOH530 |
B | ARG11 |
B | ILE12 |
B | ASN35 |
B | ASP36 |
B | LEU37 |
B | ARG80 |
B | CYS98 |
site_id | AC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD C 901 |
Chain | Residue |
C | GLY8 |
C | TYR9 |
C | GLY10 |
C | ARG11 |
C | ILE12 |
C | ASN35 |
C | ASP36 |
C | ARG80 |
C | CYS98 |
C | THR99 |
C | GLY100 |
C | SER122 |
C | ALA123 |
C | CYS154 |
C | ASN185 |
C | ASN316 |
C | PHE320 |
C | HOH337 |
C | HOH341 |
C | HOH343 |
C | HOH364 |
C | HOH365 |
C | HOH369 |
C | HOH372 |
C | HOH383 |
C | HOH384 |
C | HOH395 |
D | VAL192 |
D | TYR193 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE NAD D 901 |
Chain | Residue |
C | VAL192 |
D | GLY10 |
D | ARG11 |
D | ILE12 |
D | ASP36 |
D | CYS98 |
D | THR99 |
D | SER122 |
D | CYS154 |
D | ASN185 |
D | ASN316 |
D | HOH344 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE NAD E 901 |
Chain | Residue |
E | GLY8 |
E | GLY10 |
E | ARG11 |
E | ILE12 |
E | ASP36 |
E | CYS98 |
E | PHE101 |
E | SER122 |
E | CYS154 |
E | ASN185 |
E | ASN316 |
E | PHE320 |
E | HOH352 |
F | VAL192 |
site_id | AC5 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAD F 901 |
Chain | Residue |
F | HOH344 |
F | HOH349 |
F | HOH350 |
F | HOH473 |
F | GLY8 |
F | GLY10 |
F | ARG11 |
F | ILE12 |
F | ASN35 |
F | ASP36 |
F | LEU37 |
F | ARG80 |
F | CYS98 |
F | THR99 |
F | GLY100 |
F | SER122 |
F | ALA123 |
F | CYS154 |
F | ASN185 |
F | ASN316 |
F | PHE320 |
F | HOH338 |
F | HOH339 |
F | HOH341 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAD G 901 |
Chain | Residue |
G | ASN7 |
G | GLY8 |
G | GLY10 |
G | ARG11 |
G | ILE12 |
G | ASP36 |
G | ARG80 |
G | CYS98 |
G | THR99 |
G | GLY100 |
G | SER122 |
G | ALA123 |
G | THR184 |
G | ASN185 |
G | ASN316 |
G | HOH343 |
G | HOH344 |
G | HOH355 |
G | HOH487 |
site_id | AC7 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD H 901 |
Chain | Residue |
G | VAL192 |
H | GLY8 |
H | TYR9 |
H | GLY10 |
H | ARG11 |
H | ILE12 |
H | ASN35 |
H | ASP36 |
H | LEU37 |
H | ARG80 |
H | CYS98 |
H | THR99 |
H | GLY100 |
H | SER122 |
H | ALA123 |
H | CYS154 |
H | THR184 |
H | ASN185 |
H | ASN316 |
H | PHE320 |
H | HOH341 |
H | HOH353 |
H | HOH355 |
H | HOH356 |
H | HOH360 |
H | HOH380 |
H | HOH499 |
H | HOH527 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
A | ALA152-LEU159 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
A | HIS181 | |
A | CYS154 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
B | HIS181 | |
B | CYS154 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
C | HIS181 | |
C | CYS154 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
D | HIS181 | |
D | CYS154 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
E | HIS181 | |
E | CYS154 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
F | HIS181 | |
F | CYS154 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
G | HIS181 | |
G | CYS154 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1szj |
Chain | Residue | Details |
H | HIS181 | |
H | CYS154 |