6ITE
Crystal structure of group A Streptococcal surface dehydrogenase (SDH)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| O | 0000166 | molecular_function | nucleotide binding |
| O | 0002020 | molecular_function | protease binding |
| O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| O | 0005737 | cellular_component | cytoplasm |
| O | 0006006 | biological_process | glucose metabolic process |
| O | 0006096 | biological_process | glycolytic process |
| O | 0016491 | molecular_function | oxidoreductase activity |
| O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| O | 0050661 | molecular_function | NADP binding |
| O | 0051287 | molecular_function | NAD binding |
| P | 0000166 | molecular_function | nucleotide binding |
| P | 0002020 | molecular_function | protease binding |
| P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| P | 0005737 | cellular_component | cytoplasm |
| P | 0006006 | biological_process | glucose metabolic process |
| P | 0006096 | biological_process | glycolytic process |
| P | 0016491 | molecular_function | oxidoreductase activity |
| P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| P | 0050661 | molecular_function | NADP binding |
| P | 0051287 | molecular_function | NAD binding |
| Q | 0000166 | molecular_function | nucleotide binding |
| Q | 0002020 | molecular_function | protease binding |
| Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| Q | 0005737 | cellular_component | cytoplasm |
| Q | 0006006 | biological_process | glucose metabolic process |
| Q | 0006096 | biological_process | glycolytic process |
| Q | 0016491 | molecular_function | oxidoreductase activity |
| Q | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| Q | 0050661 | molecular_function | NADP binding |
| Q | 0051287 | molecular_function | NAD binding |
| R | 0000166 | molecular_function | nucleotide binding |
| R | 0002020 | molecular_function | protease binding |
| R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| R | 0005737 | cellular_component | cytoplasm |
| R | 0006006 | biological_process | glucose metabolic process |
| R | 0006096 | biological_process | glycolytic process |
| R | 0016491 | molecular_function | oxidoreductase activity |
| R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| R | 0050661 | molecular_function | NADP binding |
| R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue NAD P 401 |
| Chain | Residue |
| P | ASN8 |
| P | ALA96 |
| P | THR97 |
| P | GLY98 |
| P | PHE99 |
| P | PHE100 |
| P | THR121 |
| P | ALA122 |
| P | ASN316 |
| P | TYR320 |
| P | SO4402 |
| P | GLY9 |
| P | HOH520 |
| P | HOH535 |
| P | HOH549 |
| P | HOH567 |
| P | HOH581 |
| P | HOH583 |
| P | HOH587 |
| P | HOH604 |
| P | HOH625 |
| P | HOH656 |
| P | GLY11 |
| P | HOH658 |
| P | HOH663 |
| P | HOH681 |
| P | HOH724 |
| Q | PRO191 |
| Q | HOH560 |
| P | ARG12 |
| P | ILE13 |
| P | ASN33 |
| P | ASP34 |
| P | LEU35 |
| P | ARG78 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 P 402 |
| Chain | Residue |
| P | THR182 |
| P | ASP184 |
| P | ARG199 |
| P | ARG235 |
| P | NAD401 |
| P | HOH535 |
| P | HOH658 |
| P | HOH661 |
| P | HOH694 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | binding site for residue NAD Q 401 |
| Chain | Residue |
| P | PRO191 |
| P | HOH559 |
| Q | ASN8 |
| Q | GLY9 |
| Q | GLY11 |
| Q | ARG12 |
| Q | ILE13 |
| Q | ASN33 |
| Q | ASP34 |
| Q | LEU35 |
| Q | GLU77 |
| Q | ARG78 |
| Q | ALA96 |
| Q | THR97 |
| Q | GLY98 |
| Q | PHE99 |
| Q | PHE100 |
| Q | THR121 |
| Q | ALA122 |
| Q | ASN316 |
| Q | TYR320 |
| Q | SO4402 |
| Q | HOH516 |
| Q | HOH540 |
| Q | HOH564 |
| Q | HOH566 |
| Q | HOH577 |
| Q | HOH587 |
| Q | HOH591 |
| Q | HOH596 |
| Q | HOH601 |
| Q | HOH621 |
| Q | HOH641 |
| Q | HOH646 |
| Q | HOH651 |
| Q | HOH702 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 Q 402 |
| Chain | Residue |
| Q | THR182 |
| Q | ASP184 |
| Q | ARG199 |
| Q | ARG235 |
| Q | NAD401 |
| Q | HOH566 |
| Q | HOH580 |
| Q | HOH628 |
| Q | HOH636 |
| Q | HOH641 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 Q 403 |
| Chain | Residue |
| Q | LYS172 |
| Q | HOH505 |
| Q | HOH530 |
| Q | HOH538 |
| R | LYS172 |
| site_id | AC6 |
| Number of Residues | 33 |
| Details | binding site for residue NAD R 401 |
| Chain | Residue |
| R | GLY11 |
| R | ARG12 |
| R | ILE13 |
| R | ASN33 |
| R | ASP34 |
| R | LEU35 |
| R | GLU77 |
| R | ARG78 |
| R | ALA96 |
| R | THR97 |
| R | GLY98 |
| R | PHE99 |
| R | PHE100 |
| R | THR121 |
| R | ALA122 |
| R | ASN316 |
| R | TYR320 |
| R | SO4402 |
| R | HOH514 |
| R | HOH518 |
| R | HOH526 |
| R | HOH531 |
| R | HOH546 |
| R | HOH568 |
| R | HOH588 |
| R | HOH600 |
| R | HOH622 |
| R | HOH629 |
| R | HOH642 |
| O | PRO191 |
| O | HOH535 |
| R | ASN8 |
| R | GLY9 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 R 402 |
| Chain | Residue |
| R | THR182 |
| R | ARG199 |
| R | ARG235 |
| R | NAD401 |
| R | HOH517 |
| R | HOH591 |
| site_id | AC8 |
| Number of Residues | 35 |
| Details | binding site for residue NAD O 401 |
| Chain | Residue |
| O | ASN8 |
| O | GLY9 |
| O | GLY11 |
| O | ARG12 |
| O | ILE13 |
| O | ASN33 |
| O | ASP34 |
| O | LEU35 |
| O | GLU77 |
| O | ARG78 |
| O | ALA96 |
| O | THR97 |
| O | GLY98 |
| O | PHE99 |
| O | PHE100 |
| O | THR121 |
| O | ALA122 |
| O | ASN316 |
| O | TYR320 |
| O | SO4402 |
| O | HOH514 |
| O | HOH537 |
| O | HOH546 |
| O | HOH558 |
| O | HOH562 |
| O | HOH572 |
| O | HOH590 |
| O | HOH597 |
| O | HOH617 |
| O | HOH638 |
| O | HOH645 |
| O | HOH646 |
| O | HOH677 |
| R | PRO191 |
| R | HOH569 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 O 402 |
| Chain | Residue |
| O | THR182 |
| O | ASP184 |
| O | ARG199 |
| O | ARG235 |
| O | NAD401 |
| O | HOH514 |
| O | HOH601 |
| O | HOH628 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 O 403 |
| Chain | Residue |
| O | LYS172 |
| O | HOH505 |
| O | HOH534 |
| O | HOH568 |
| P | LYS172 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| P | ALA150-LEU157 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00362","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"Q6GIL8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






