7JWK
Crystal Structure of Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) from Mycoplasma genitalium 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 | 0006735 | biological_process | NADH regeneration |
A | 0009986 | cellular_component | cell surface |
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 | 0044650 | biological_process | adhesion of symbiont to host cell |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
A | 0140032 | molecular_function | glycosylation-dependent protein 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 | 0006735 | biological_process | NADH regeneration |
B | 0009986 | cellular_component | cell surface |
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 | 0044650 | biological_process | adhesion of symbiont to host cell |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
B | 0140032 | molecular_function | glycosylation-dependent protein 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 | 0006735 | biological_process | NADH regeneration |
C | 0009986 | cellular_component | cell surface |
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 | 0044650 | biological_process | adhesion of symbiont to host cell |
C | 0050661 | molecular_function | NADP binding |
C | 0051287 | molecular_function | NAD binding |
C | 0140032 | molecular_function | glycosylation-dependent protein 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 | 0006735 | biological_process | NADH regeneration |
D | 0009986 | cellular_component | cell surface |
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 | 0044650 | biological_process | adhesion of symbiont to host cell |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
D | 0140032 | molecular_function | glycosylation-dependent protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 33 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | GLY14 |
A | SER101 |
A | THR102 |
A | GLY103 |
A | SER125 |
A | ALA126 |
A | CYS157 |
A | ALA188 |
A | ASN319 |
A | TYR323 |
A | PO4403 |
A | GLY16 |
A | HOH510 |
A | HOH512 |
A | HOH513 |
A | HOH526 |
A | HOH533 |
A | HOH552 |
A | HOH559 |
A | HOH565 |
A | HOH568 |
A | HOH575 |
A | ARG17 |
A | HOH577 |
A | HOH581 |
A | HOH592 |
A | HOH610 |
A | ILE18 |
A | ASN38 |
A | ASP39 |
A | LEU40 |
A | GLU82 |
A | LYS83 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue PO4 A 402 |
Chain | Residue |
A | SER156 |
A | CYS157 |
A | THR158 |
A | HIS184 |
A | THR215 |
A | GLY216 |
A | PO4403 |
A | HOH544 |
A | HOH563 |
A | HOH575 |
A | HOH579 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue PO4 A 403 |
Chain | Residue |
A | THR187 |
A | ARG202 |
A | ARG238 |
A | NAD401 |
A | PO4402 |
A | HOH501 |
A | HOH505 |
A | HOH526 |
A | HOH544 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue PEG A 404 |
Chain | Residue |
A | LYS275 |
A | CYS277 |
A | ASP285 |
A | SER289 |
D | TYR52 |
site_id | AC5 |
Number of Residues | 31 |
Details | binding site for residue NAD B 401 |
Chain | Residue |
B | GLY14 |
B | GLY16 |
B | ARG17 |
B | ILE18 |
B | ASP39 |
B | LEU40 |
B | LYS83 |
B | SER101 |
B | THR102 |
B | GLY103 |
B | ARG104 |
B | PHE105 |
B | SER125 |
B | ALA126 |
B | CYS157 |
B | ALA188 |
B | ASN319 |
B | TYR323 |
B | PO4403 |
B | HOH508 |
B | HOH522 |
B | HOH543 |
B | HOH548 |
B | HOH549 |
B | HOH552 |
B | HOH557 |
B | HOH564 |
B | HOH587 |
B | HOH588 |
B | HOH604 |
D | HOH520 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue PO4 B 402 |
Chain | Residue |
B | SER156 |
B | CYS157 |
B | THR158 |
B | HIS184 |
B | THR215 |
B | GLY216 |
B | HOH529 |
B | HOH537 |
B | HOH551 |
B | HOH587 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue PO4 B 403 |
Chain | Residue |
B | THR187 |
B | ASP189 |
B | ARG202 |
B | ARG238 |
B | NAD401 |
B | HOH502 |
B | HOH513 |
B | HOH529 |
B | HOH545 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue PEG B 404 |
Chain | Residue |
B | LYS275 |
B | CYS277 |
B | ASP285 |
B | SER289 |
B | ILE294 |
C | TYR52 |
C | GLU58 |
site_id | AC9 |
Number of Residues | 33 |
Details | binding site for residue NAD C 401 |
Chain | Residue |
C | GLY14 |
C | GLY16 |
C | ARG17 |
C | ILE18 |
C | ASN38 |
C | ASP39 |
C | LEU40 |
C | GLU82 |
C | LYS83 |
C | SER101 |
C | THR102 |
C | GLY103 |
C | ARG104 |
C | PHE105 |
C | SER125 |
C | ALA126 |
C | CYS157 |
C | ALA188 |
C | ASN319 |
C | TYR323 |
C | PO4403 |
C | HOH520 |
C | HOH532 |
C | HOH534 |
C | HOH543 |
C | HOH544 |
C | HOH549 |
C | HOH554 |
C | HOH558 |
C | HOH563 |
C | HOH568 |
C | HOH571 |
C | HOH579 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residue PO4 C 402 |
Chain | Residue |
C | SER156 |
C | CYS157 |
C | THR158 |
C | HIS184 |
C | THR215 |
C | GLY216 |
C | HOH512 |
C | HOH523 |
C | HOH553 |
C | HOH568 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue PO4 C 403 |
Chain | Residue |
C | THR187 |
C | ASP189 |
C | ARG202 |
C | ARG238 |
C | NAD401 |
C | HOH501 |
C | HOH512 |
C | HOH526 |
C | HOH545 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue PEG C 404 |
Chain | Residue |
C | LYS275 |
C | CYS277 |
C | ASP285 |
C | SER289 |
site_id | AD4 |
Number of Residues | 26 |
Details | binding site for residue NAD D 401 |
Chain | Residue |
B | HOH519 |
D | GLY14 |
D | GLY16 |
D | ARG17 |
D | ILE18 |
D | ASN38 |
D | ASP39 |
D | LEU40 |
D | LYS83 |
D | SER101 |
D | THR102 |
D | GLY103 |
D | PHE105 |
D | SER125 |
D | ALA126 |
D | CYS157 |
D | ALA188 |
D | ASN319 |
D | PO4403 |
D | HOH503 |
D | HOH508 |
D | HOH514 |
D | HOH527 |
D | HOH528 |
D | HOH529 |
D | HOH558 |
site_id | AD5 |
Number of Residues | 10 |
Details | binding site for residue PO4 D 402 |
Chain | Residue |
D | SER156 |
D | CYS157 |
D | THR158 |
D | HIS184 |
D | THR215 |
D | GLY216 |
D | PO4403 |
D | HOH506 |
D | HOH508 |
D | HOH509 |
site_id | AD6 |
Number of Residues | 10 |
Details | binding site for residue PO4 D 403 |
Chain | Residue |
D | THR187 |
D | ASP189 |
D | ARG202 |
D | ARG238 |
D | NAD401 |
D | PO4402 |
D | HOH501 |
D | HOH506 |
D | HOH508 |
D | HOH556 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue PEG D 404 |
Chain | Residue |
D | CYS277 |
D | ASP285 |
D | SER289 |
Functional Information from PROSITE/UniProt
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 | CYS157 | |
B | CYS157 | |
C | CYS157 | |
D | CYS157 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
A | SER156 | |
A | THR187 | |
A | ARG202 | |
A | THR215 | |
A | ARG238 | |
A | ASN319 | |
B | ARG17 | |
B | ASP39 | |
B | LYS83 | |
B | SER125 | |
B | SER156 | |
B | THR187 | |
B | ARG202 | |
B | THR215 | |
B | ARG238 | |
B | ASN319 | |
C | ARG17 | |
C | ASP39 | |
C | LYS83 | |
C | SER125 | |
C | SER156 | |
C | THR187 | |
C | ARG202 | |
C | THR215 | |
C | ARG238 | |
C | ASN319 | |
D | ARG17 | |
D | ASP39 | |
D | LYS83 | |
D | SER125 | |
D | SER156 | |
D | THR187 | |
D | ARG202 | |
D | THR215 | |
D | ARG238 | |
D | ASN319 | |
A | ASP39 | |
A | LYS83 | |
A | SER125 | |
A | ARG17 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
D | HIS184 | |
A | HIS184 | |
B | HIS184 | |
C | HIS184 |