6X2E
Crystal Structure of Chlamydia trachomatis mixed (apo/holo) Glyceraldehyde 3-phosphate dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006006 | biological_process | glucose metabolic process |
A | 0006096 | biological_process | glycolytic 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 | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006006 | biological_process | glucose metabolic process |
B | 0006096 | biological_process | glycolytic 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 | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006006 | biological_process | glucose metabolic process |
C | 0006096 | biological_process | glycolytic 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 | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006006 | biological_process | glucose metabolic process |
D | 0006096 | biological_process | glycolytic 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 | 29 |
Details | binding site for residue NAD A 400 |
Chain | Residue |
A | GLY7 |
A | GLY97 |
A | LEU98 |
A | THR119 |
A | ALA120 |
A | CYS150 |
A | ALA181 |
A | ASN314 |
A | TYR318 |
A | HOH529 |
A | HOH531 |
A | PHE8 |
A | HOH534 |
A | HOH549 |
A | HOH553 |
A | HOH556 |
A | HOH578 |
A | HOH585 |
A | HOH592 |
A | HOH628 |
A | HOH659 |
C | HOH546 |
A | GLY9 |
A | ARG10 |
A | ILE11 |
A | ASP33 |
A | LEU34 |
A | SER95 |
A | THR96 |
site_id | AC2 |
Number of Residues | 32 |
Details | binding site for residue NAD C 400 |
Chain | Residue |
C | GLY7 |
C | PHE8 |
C | GLY9 |
C | ARG10 |
C | ILE11 |
C | ASN32 |
C | ASP33 |
C | LEU34 |
C | LYS77 |
C | SER95 |
C | THR96 |
C | GLY97 |
C | LEU98 |
C | THR119 |
C | ALA120 |
C | ALA181 |
C | ASN314 |
C | TYR318 |
C | HOH507 |
C | HOH526 |
C | HOH537 |
C | HOH552 |
C | HOH568 |
C | HOH575 |
C | HOH578 |
C | HOH579 |
C | HOH583 |
C | HOH589 |
C | HOH597 |
C | HOH599 |
C | HOH637 |
C | HOH643 |
site_id | AC3 |
Number of Residues | 23 |
Details | binding site for residue NAD D 400 |
Chain | Residue |
D | GLY7 |
D | PHE8 |
D | GLY9 |
D | ARG10 |
D | ILE11 |
D | ASP33 |
D | LEU34 |
D | SER95 |
D | THR96 |
D | GLY97 |
D | LEU98 |
D | THR119 |
D | ALA120 |
D | CYS150 |
D | ALA181 |
D | ASN314 |
D | TYR318 |
D | HOH527 |
D | HOH543 |
D | HOH547 |
D | HOH556 |
D | HOH568 |
D | HOH624 |
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 | ALA148-LEU155 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
A | CYS150 | |
B | CYS150 | |
C | CYS150 | |
D | CYS150 |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
A | ARG10 | |
B | ARG10 | |
B | ASP33 | |
B | LYS77 | |
B | THR119 | |
B | SER149 | |
B | THR180 | |
B | THR209 | |
B | ARG232 | |
B | ASN314 | |
C | ARG10 | |
A | ASP33 | |
C | ASP33 | |
C | LYS77 | |
C | THR119 | |
C | SER149 | |
C | THR180 | |
C | THR209 | |
C | ARG232 | |
C | ASN314 | |
D | ARG10 | |
D | ASP33 | |
A | LYS77 | |
D | LYS77 | |
D | THR119 | |
D | SER149 | |
D | THR180 | |
D | THR209 | |
D | ARG232 | |
D | ASN314 | |
A | THR119 | |
A | SER149 | |
A | THR180 | |
A | THR209 | |
A | ARG232 | |
A | ASN314 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
A | HIS177 | |
B | HIS177 | |
C | HIS177 | |
D | HIS177 |