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 | 0006735 | biological_process | NADH regeneration |
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 | 0006735 | biological_process | NADH regeneration |
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 | 0006735 | biological_process | NADH regeneration |
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 | 0006735 | biological_process | NADH regeneration |
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 | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
P | CYS152 | |
Q | CYS152 | |
R | CYS152 | |
O | CYS152 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00362 |
Chain | Residue | Details |
P | ARG12 | |
P | ASN316 | |
Q | ARG12 | |
Q | ASP34 | |
Q | ARG78 | |
Q | THR121 | |
Q | SER151 | |
Q | THR182 | |
Q | ARG199 | |
Q | THR212 | |
Q | ARG235 | |
P | ASP34 | |
Q | ASN316 | |
R | ARG12 | |
R | ASP34 | |
R | ARG78 | |
R | THR121 | |
R | SER151 | |
R | THR182 | |
R | ARG199 | |
R | THR212 | |
R | ARG235 | |
P | ARG78 | |
R | ASN316 | |
O | ARG12 | |
O | ASP34 | |
O | ARG78 | |
O | THR121 | |
O | SER151 | |
O | THR182 | |
O | ARG199 | |
O | THR212 | |
O | ARG235 | |
P | THR121 | |
O | ASN316 | |
P | SER151 | |
P | THR182 | |
P | ARG199 | |
P | THR212 | |
P | ARG235 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Activates thiol group during catalysis => ECO:0000250|UniProtKB:Q6GIL8 |
Chain | Residue | Details |
P | HIS179 | |
Q | HIS179 | |
R | HIS179 | |
O | HIS179 |