7C5L
Crystal Structure of C150S mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli at 2.1 Angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
O | 0000166 | molecular_function | nucleotide binding |
O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
O | 0006006 | biological_process | glucose metabolic 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 | 0042802 | molecular_function | identical protein binding |
O | 0050661 | molecular_function | NADP binding |
O | 0051287 | molecular_function | NAD binding |
P | 0000166 | molecular_function | nucleotide binding |
P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
P | 0006006 | biological_process | glucose metabolic 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 | 0042802 | molecular_function | identical protein binding |
P | 0050661 | molecular_function | NADP binding |
P | 0051287 | molecular_function | NAD binding |
Q | 0000166 | molecular_function | nucleotide binding |
Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
Q | 0006006 | biological_process | glucose metabolic 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 | 0042802 | molecular_function | identical protein binding |
Q | 0050661 | molecular_function | NADP binding |
Q | 0051287 | molecular_function | NAD binding |
R | 0000166 | molecular_function | nucleotide binding |
R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
R | 0006006 | biological_process | glucose metabolic 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 | 0042802 | molecular_function | identical protein binding |
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 O 401 |
Chain | Residue |
O | ASN7 |
O | LYS78 |
O | CYS96 |
O | THR97 |
O | GLY98 |
O | PHE99 |
O | SER120 |
O | ALA121 |
O | SER150 |
O | THR180 |
O | ASN315 |
O | GLY8 |
O | PHE319 |
O | HOH506 |
O | HOH513 |
O | HOH516 |
O | HOH528 |
O | HOH535 |
O | HOH559 |
O | HOH595 |
O | HOH616 |
O | HOH629 |
O | PHE9 |
O | HOH645 |
O | HOH657 |
O | HOH659 |
O | HOH662 |
O | HOH676 |
O | HOH706 |
O | GLY10 |
O | ARG11 |
O | ILE12 |
O | ASN33 |
O | ASP34 |
O | LEU35 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue CL O 402 |
Chain | Residue |
O | ALA80 |
O | LYS81 |
O | ALA108 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CL O 403 |
Chain | Residue |
O | HIS177 |
O | HIS207 |
O | ALA230 |
O | ARG232 |
O | HOH614 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue PO4 O 404 |
Chain | Residue |
O | ALA201 |
O | HOH546 |
O | HOH589 |
P | ALA201 |
P | HOH654 |
Q | ALA201 |
R | ALA201 |
site_id | AC5 |
Number of Residues | 34 |
Details | binding site for residue NAD P 401 |
Chain | Residue |
P | ASN7 |
P | GLY8 |
P | PHE9 |
P | GLY10 |
P | ARG11 |
P | ILE12 |
P | ASN33 |
P | ASP34 |
P | LEU35 |
P | LYS78 |
P | CYS96 |
P | THR97 |
P | GLY98 |
P | PHE99 |
P | SER120 |
P | ALA121 |
P | SER150 |
P | THR180 |
P | ASN315 |
P | PHE319 |
P | HOH509 |
P | HOH517 |
P | HOH520 |
P | HOH526 |
P | HOH531 |
P | HOH576 |
P | HOH607 |
P | HOH627 |
P | HOH655 |
P | HOH661 |
P | HOH662 |
P | HOH673 |
P | HOH704 |
P | HOH705 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue CL P 402 |
Chain | Residue |
P | HIS177 |
P | HIS207 |
P | ALA230 |
P | ARG232 |
P | HOH643 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue EDO P 403 |
Chain | Residue |
P | ARG18 |
P | GLU22 |
P | HOH641 |
site_id | AC8 |
Number of Residues | 33 |
Details | binding site for residue NAD Q 401 |
Chain | Residue |
Q | ASP34 |
Q | LEU35 |
Q | LYS78 |
Q | CYS96 |
Q | THR97 |
Q | GLY98 |
Q | PHE99 |
Q | SER120 |
Q | ALA121 |
Q | SER150 |
Q | THR180 |
Q | ASN315 |
Q | PHE319 |
Q | HOH514 |
Q | HOH519 |
Q | HOH521 |
Q | HOH527 |
Q | HOH538 |
Q | HOH600 |
Q | HOH605 |
Q | HOH615 |
Q | HOH621 |
Q | HOH644 |
Q | HOH655 |
Q | HOH668 |
Q | HOH684 |
P | HOH561 |
Q | ASN7 |
Q | GLY8 |
Q | GLY10 |
Q | ARG11 |
Q | ILE12 |
Q | ASN33 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue CL Q 402 |
Chain | Residue |
Q | HIS177 |
Q | HIS207 |
Q | ALA230 |
Q | ARG232 |
Q | HOH534 |
site_id | AD1 |
Number of Residues | 33 |
Details | binding site for residue NAD R 401 |
Chain | Residue |
R | ASN7 |
R | GLY8 |
R | PHE9 |
R | GLY10 |
R | ARG11 |
R | ILE12 |
R | ASN33 |
R | ASP34 |
R | LEU35 |
R | LYS78 |
R | CYS96 |
R | THR97 |
R | GLY98 |
R | PHE99 |
R | SER120 |
R | ALA121 |
R | SER150 |
R | ASN315 |
R | PHE319 |
R | HOH502 |
R | HOH511 |
R | HOH514 |
R | HOH542 |
R | HOH550 |
R | HOH554 |
R | HOH573 |
R | HOH578 |
R | HOH580 |
R | HOH585 |
R | HOH593 |
R | HOH607 |
R | HOH619 |
R | HOH625 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue CL R 402 |
Chain | Residue |
R | HIS177 |
R | HIS207 |
R | ALA230 |
R | ARG232 |
R | HOH557 |
Functional Information from PROSITE/UniProt
site_id | PS00430 |
Number of Residues | 89 |
Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. hhhhhhssglvprgshmasmskvgingfgrigrlvlrrllevksnidvvaindltspkilayllkhdsnygpfpwsvdfte..................................DSLIVDGK |
Chain | Residue | Details |
O | HIS-18-LYS70 |