7C5O
Crystal Structure of H177A mutant of Glyceraldehyde-3-phosphate-dehydrogenase1 from Escherichia coli complexed with NAD at 1.98 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 | 31 |
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 | CYS150 |
O | ASN315 |
O | PHE319 |
O | GLY8 |
O | HOH511 |
O | HOH514 |
O | HOH524 |
O | HOH594 |
O | HOH633 |
O | HOH653 |
O | HOH656 |
O | HOH667 |
O | HOH677 |
O | HOH690 |
O | PHE9 |
O | HOH694 |
O | HOH708 |
O | GLY10 |
O | ARG11 |
O | ILE12 |
O | ASN33 |
O | ASP34 |
O | LEU35 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue PO4 O 402 |
Chain | Residue |
O | ALA201 |
O | HOH574 |
P | ALA201 |
Q | ALA201 |
R | ALA201 |
R | HOH610 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue CL O 403 |
Chain | Residue |
O | LYS213 |
O | LYS227 |
O | GLY228 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CL O 404 |
Chain | Residue |
O | ALA80 |
O | LYS81 |
O | ALA108 |
O | HOH582 |
O | HOH768 |
O | HOH820 |
site_id | AC5 |
Number of Residues | 31 |
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 | PHE99 |
P | SER120 |
P | ALA121 |
P | CYS150 |
P | ASN315 |
P | PHE319 |
P | HOH502 |
P | HOH508 |
P | HOH512 |
P | HOH591 |
P | HOH602 |
P | HOH616 |
P | HOH620 |
P | HOH628 |
P | HOH631 |
P | HOH634 |
P | HOH653 |
P | HOH695 |
Q | HOH562 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CL P 402 |
Chain | Residue |
P | LYS213 |
P | LYS227 |
P | GLY228 |
P | HOH775 |
site_id | AC7 |
Number of Residues | 31 |
Details | binding site for residue NAD Q 401 |
Chain | Residue |
Q | HOH537 |
Q | HOH548 |
Q | HOH567 |
Q | HOH574 |
Q | HOH585 |
Q | HOH607 |
Q | HOH618 |
Q | HOH620 |
Q | HOH633 |
Q | HOH648 |
Q | HOH674 |
Q | HOH678 |
Q | HOH679 |
Q | ASN7 |
Q | GLY8 |
Q | GLY10 |
Q | ARG11 |
Q | ILE12 |
Q | ASN33 |
Q | ASP34 |
Q | LEU35 |
Q | LYS78 |
Q | CYS96 |
Q | THR97 |
Q | GLY98 |
Q | PHE99 |
Q | SER120 |
Q | ALA121 |
Q | CYS150 |
Q | ASN315 |
Q | PHE319 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue CL Q 402 |
Chain | Residue |
Q | LYS227 |
Q | GLY228 |
Q | HOH774 |
site_id | AC9 |
Number of Residues | 27 |
Details | binding site for residue NAD R 401 |
Chain | Residue |
R | GLY8 |
R | GLY10 |
R | ARG11 |
R | ILE12 |
R | ASP34 |
R | LEU35 |
R | LYS78 |
R | CYS96 |
R | THR97 |
R | GLY98 |
R | PHE99 |
R | SER120 |
R | ALA121 |
R | CYS150 |
R | ASN315 |
R | PHE319 |
R | HOH512 |
R | HOH520 |
R | HOH537 |
R | HOH539 |
R | HOH544 |
R | HOH570 |
R | HOH573 |
R | HOH584 |
R | HOH605 |
R | HOH607 |
R | HOH632 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue CL R 402 |
Chain | Residue |
R | LYS227 |
R | GLY228 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
O | ALA148-LEU155 |
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 |