3DOC
Crystal Structure of TrkA glyceraldehyde-3-phosphate dehydrogenase from Brucella melitensis
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NAD A 901 |
| Chain | Residue |
| A | GLY9 |
| A | ASN316 |
| A | GLU317 |
| A | PHE320 |
| A | PHE10 |
| A | GLY11 |
| A | ARG12 |
| A | ILE13 |
| A | ASP36 |
| A | SER122 |
| A | ALA123 |
| A | CYS153 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAD B 901 |
| Chain | Residue |
| B | GLY9 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASN35 |
| B | ASP36 |
| B | ARG80 |
| B | CYS98 |
| B | THR99 |
| B | GLY100 |
| B | SER122 |
| B | ALA123 |
| B | CYS153 |
| B | ASN316 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAD D 901 |
| Chain | Residue |
| D | GLY9 |
| D | GLY11 |
| D | ARG12 |
| D | ILE13 |
| D | ASN35 |
| D | ASP36 |
| D | LEU37 |
| D | ARG80 |
| D | CYS98 |
| D | THR99 |
| D | GLY100 |
| D | SER122 |
| D | ALA123 |
| D | ASN316 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAD C 901 |
| Chain | Residue |
| C | GLY9 |
| C | GLY11 |
| C | ARG12 |
| C | ILE13 |
| C | ASN35 |
| C | ASP36 |
| C | LEU37 |
| C | ARG80 |
| C | CYS98 |
| C | THR99 |
| C | GLY100 |
| C | SER122 |
| C | ALA123 |
| C | CYS153 |
| C | ASN316 |
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 | ALA151-LEU158 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| A | HIS180 | |
| A | CYS153 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| B | HIS180 | |
| B | CYS153 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| C | HIS180 | |
| C | CYS153 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| D | HIS180 | |
| D | CYS153 |
