6OK4
Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Chlamydia trachomatis with bound NAD
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 | 27 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | GLY7 |
A | THR96 |
A | GLY97 |
A | LEU98 |
A | THR119 |
A | ALA120 |
A | CYS150 |
A | ALA181 |
A | ASN314 |
A | TYR318 |
A | HOH507 |
A | PHE8 |
A | HOH519 |
A | HOH538 |
A | HOH543 |
A | HOH549 |
A | HOH561 |
A | HOH571 |
A | HOH576 |
C | HOH514 |
A | GLY9 |
A | ARG10 |
A | ILE11 |
A | ASN32 |
A | ASP33 |
A | LEU34 |
A | SER95 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | THR128 |
A | ASN134 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | LYS246 |
A | HOH539 |
B | GLU170 |
C | ARG304 |
C | EDO404 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue PO4 A 404 |
Chain | Residue |
A | SER149 |
A | THR151 |
A | THR209 |
A | GLY210 |
A | ALA211 |
A | HOH509 |
A | HOH530 |
A | HOH537 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue PO4 A 405 |
Chain | Residue |
A | GLU170 |
A | LYS246 |
A | ARG304 |
A | HOH559 |
B | LYS246 |
C | GLU169 |
C | ARG304 |
C | PO4407 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | THR49 |
A | ILE285 |
C | HOH569 |
D | THR49 |
D | ILE285 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue PEG A 407 |
Chain | Residue |
A | GLY132 |
A | VAL133 |
A | ASN134 |
A | HIS135 |
A | GLN136 |
A | GLN137 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue CL A 408 |
Chain | Residue |
A | HIS-1 |
A | HIS0 |
site_id | AC9 |
Number of Residues | 21 |
Details | binding site for residue NAD B 401 |
Chain | Residue |
B | GLY7 |
B | GLY9 |
B | ARG10 |
B | ILE11 |
B | ASN32 |
B | ASP33 |
B | LEU34 |
B | SER95 |
B | THR96 |
B | GLY97 |
B | LEU98 |
B | THR119 |
B | ALA120 |
B | CYS150 |
B | ALA181 |
B | ASN314 |
B | TYR318 |
B | HOH534 |
B | HOH536 |
B | HOH553 |
D | HOH542 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO B 402 |
Chain | Residue |
B | ASN165 |
B | ALA259 |
B | HIS262 |
B | ALA263 |
B | HOH540 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | LEU163 |
B | GLY167 |
B | ILE168 |
B | GLU221 |
B | LYS225 |
B | SER248 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | HOH504 |
C | ASP164 |
C | ASN165 |
C | PHE166 |
B | SER248 |
B | SER249 |
B | ALA250 |
B | ARG304 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | TYR253 |
B | GLY298 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
A | GLN296 |
B | ASP193 |
B | ARG195 |
B | HOH503 |
B | HOH561 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue PO4 B 407 |
Chain | Residue |
B | SER149 |
B | THR151 |
B | THR209 |
B | GLY210 |
B | ALA211 |
B | HOH545 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue PEG B 408 |
Chain | Residue |
B | VAL133 |
B | ASN134 |
B | HIS135 |
B | GLN136 |
B | GLN137 |
site_id | AD8 |
Number of Residues | 24 |
Details | binding site for residue NAD C 401 |
Chain | Residue |
C | GLY7 |
C | PHE8 |
C | GLY9 |
C | ARG10 |
C | ILE11 |
C | ASN32 |
C | ASP33 |
C | LEU34 |
C | SER95 |
C | THR96 |
C | GLY97 |
C | LEU98 |
C | THR119 |
C | ALA120 |
C | CYS150 |
C | ALA181 |
C | ASN314 |
C | TYR318 |
C | HOH506 |
C | HOH526 |
C | HOH542 |
C | HOH549 |
C | HOH557 |
C | HOH561 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue EDO C 402 |
Chain | Residue |
A | VAL35 |
C | PRO189 |
C | SER190 |
C | ARG191 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue EDO C 403 |
Chain | Residue |
C | ASP193 |
C | TRP194 |
C | HOH545 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue EDO C 404 |
Chain | Residue |
A | ARG304 |
A | EDO403 |
C | LYS246 |
C | ASP303 |
C | ARG304 |
site_id | AE3 |
Number of Residues | 1 |
Details | binding site for residue EDO C 405 |
Chain | Residue |
C | GLN296 |
site_id | AE4 |
Number of Residues | 6 |
Details | binding site for residue PO4 C 406 |
Chain | Residue |
C | SER149 |
C | THR151 |
C | THR209 |
C | GLY210 |
C | ALA211 |
C | HOH518 |
site_id | AE5 |
Number of Residues | 7 |
Details | binding site for residue PO4 C 407 |
Chain | Residue |
A | GLU169 |
A | ARG304 |
A | PO4405 |
C | GLU170 |
C | LYS246 |
C | ARG304 |
D | LYS246 |
site_id | AE6 |
Number of Residues | 1 |
Details | binding site for residue EDO C 408 |
Chain | Residue |
C | ALA300 |
site_id | AE7 |
Number of Residues | 6 |
Details | binding site for residue PEG C 409 |
Chain | Residue |
C | GLY132 |
C | VAL133 |
C | ASN134 |
C | HIS135 |
C | GLN136 |
C | GLN137 |
site_id | AE8 |
Number of Residues | 21 |
Details | binding site for residue NAD D 401 |
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 | HOH510 |
D | HOH533 |
D | HOH543 |
D | HOH583 |
site_id | AE9 |
Number of Residues | 2 |
Details | binding site for residue EDO D 402 |
Chain | Residue |
D | THR128 |
D | ASN134 |
site_id | AF1 |
Number of Residues | 8 |
Details | binding site for residue EDO D 403 |
Chain | Residue |
A | ASP164 |
A | ASN165 |
A | PHE166 |
D | SER248 |
D | SER249 |
D | ALA250 |
D | ARG304 |
D | HOH560 |
site_id | AF2 |
Number of Residues | 7 |
Details | binding site for residue PO4 D 404 |
Chain | Residue |
D | SER149 |
D | THR151 |
D | THR209 |
D | GLY210 |
D | ALA211 |
D | HOH503 |
D | HOH538 |
site_id | AF3 |
Number of Residues | 5 |
Details | binding site for residue PEG D 405 |
Chain | Residue |
D | VAL133 |
D | ASN134 |
D | HIS135 |
D | GLN136 |
D | GLN137 |
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 |