7C5N
Crystal Structure of C150A+H177A mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli at 2.0 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 | 0005737 | cellular_component | cytoplasm |
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 | 0005737 | cellular_component | cytoplasm |
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 | 0005737 | cellular_component | cytoplasm |
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 | 0005737 | cellular_component | cytoplasm |
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 | ALA150 |
O | ASN315 |
O | PHE319 |
O | GLY8 |
O | CL405 |
O | HOH507 |
O | HOH513 |
O | HOH564 |
O | HOH576 |
O | HOH581 |
O | HOH587 |
O | HOH601 |
O | HOH607 |
O | HOH609 |
O | PHE9 |
O | HOH612 |
O | HOH644 |
O | HOH661 |
O | HOH668 |
O | HOH669 |
O | HOH673 |
O | GLY10 |
O | ARG11 |
O | ILE12 |
O | ASN33 |
O | ASP34 |
O | LEU35 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue PO4 O 402 |
Chain | Residue |
O | ALA201 |
O | HOH616 |
O | HOH636 |
P | ALA201 |
P | HOH645 |
Q | ALA201 |
R | ALA201 |
R | HOH603 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CL O 403 |
Chain | Residue |
O | LYS227 |
O | GLY228 |
O | HOH733 |
O | HOH797 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue CL O 404 |
Chain | Residue |
O | ALA80 |
O | LYS81 |
O | ALA108 |
O | HOH771 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CL O 405 |
Chain | Residue |
O | THR180 |
O | NAD401 |
O | HOH646 |
site_id | AC6 |
Number of Residues | 30 |
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 | LYS78 |
P | CYS96 |
P | THR97 |
P | GLY98 |
P | SER120 |
P | ALA121 |
P | ALA150 |
P | THR180 |
P | ASN315 |
P | PHE319 |
P | CL404 |
P | HOH502 |
P | HOH523 |
P | HOH543 |
P | HOH597 |
P | HOH602 |
P | HOH610 |
P | HOH622 |
P | HOH629 |
P | HOH640 |
P | HOH655 |
P | HOH684 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue EDO P 402 |
Chain | Residue |
P | GLU62 |
P | HOH522 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue CL P 403 |
Chain | Residue |
P | LYS227 |
P | GLY228 |
P | HOH775 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue CL P 404 |
Chain | Residue |
P | THR180 |
P | NAD401 |
P | HOH603 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue CL P 405 |
Chain | Residue |
P | ALA80 |
P | LYS81 |
P | ALA108 |
P | HOH714 |
site_id | AD2 |
Number of Residues | 33 |
Details | binding site for residue NAD Q 401 |
Chain | Residue |
Q | ARG11 |
Q | ILE12 |
Q | ASN33 |
Q | ASP34 |
Q | LYS78 |
Q | CYS96 |
Q | THR97 |
Q | GLY98 |
Q | PHE99 |
Q | SER120 |
Q | ALA121 |
Q | ALA150 |
Q | THR180 |
Q | ASN315 |
Q | PHE319 |
Q | CL404 |
Q | HOH519 |
Q | HOH524 |
Q | HOH552 |
Q | HOH581 |
Q | HOH584 |
Q | HOH591 |
Q | HOH596 |
Q | HOH604 |
Q | HOH615 |
Q | HOH618 |
Q | HOH621 |
Q | HOH622 |
Q | HOH641 |
Q | HOH643 |
Q | ASN7 |
Q | GLY8 |
Q | GLY10 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue CL Q 402 |
Chain | Residue |
Q | LYS227 |
Q | GLY228 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue CL Q 403 |
Chain | Residue |
Q | ALA80 |
Q | LYS81 |
Q | HOH716 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue CL Q 404 |
Chain | Residue |
Q | THR180 |
Q | NAD401 |
Q | HOH535 |
site_id | AD6 |
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 | ALA150 |
R | THR180 |
R | ASN315 |
R | PHE319 |
R | HOH513 |
R | HOH521 |
R | HOH530 |
R | HOH550 |
R | HOH567 |
R | HOH586 |
R | HOH587 |
R | HOH600 |
R | HOH604 |
R | HOH609 |
R | HOH625 |
R | HOH662 |
R | HOH666 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue CL R 402 |
Chain | Residue |
Q | HOH571 |
R | LYS227 |
R | GLY228 |
R | HOH675 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue CL R 403 |
Chain | Residue |
R | THR180 |
R | THR182 |
R | HOH550 |
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 |