7C5F
Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli at 1.88 Angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
O | 0006006 | biological_process | glucose metabolic process |
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 | 0006006 | biological_process | glucose metabolic process |
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 | 0006006 | biological_process | glucose metabolic process |
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 | 0006006 | biological_process | glucose metabolic process |
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 | 32 |
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 | THR180 |
O | ASN315 |
O | GLY8 |
O | PHE319 |
O | HOH502 |
O | HOH504 |
O | HOH511 |
O | HOH516 |
O | HOH522 |
O | HOH529 |
O | HOH580 |
O | HOH582 |
O | HOH587 |
O | PHE9 |
O | HOH601 |
O | HOH605 |
O | HOH630 |
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 | HOH572 |
O | HOH584 |
O | HOH590 |
P | ALA201 |
Q | ALA201 |
R | ALA201 |
R | HOH529 |
site_id | AC3 |
Number of Residues | 32 |
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 | CYS150 |
P | THR180 |
P | ASN315 |
P | PHE319 |
P | HOH502 |
P | HOH504 |
P | HOH505 |
P | HOH514 |
P | HOH535 |
P | HOH551 |
P | HOH555 |
P | HOH574 |
P | HOH591 |
P | HOH595 |
P | HOH600 |
P | HOH620 |
site_id | AC4 |
Number of Residues | 29 |
Details | binding site for residue NAD Q 401 |
Chain | Residue |
Q | HOH610 |
Q | HOH618 |
Q | ASN7 |
Q | GLY8 |
Q | GLY10 |
Q | ARG11 |
Q | ILE12 |
Q | ASN33 |
Q | ASP34 |
Q | LYS78 |
Q | CYS96 |
Q | THR97 |
Q | GLY98 |
Q | PHE99 |
Q | SER120 |
Q | ALA121 |
Q | CYS150 |
Q | THR180 |
Q | ASN315 |
Q | PHE319 |
Q | HOH521 |
Q | HOH527 |
Q | HOH530 |
Q | HOH532 |
Q | HOH549 |
Q | HOH563 |
Q | HOH575 |
Q | HOH577 |
Q | HOH594 |
site_id | AC5 |
Number of Residues | 25 |
Details | binding site for residue NAD R 401 |
Chain | Residue |
R | GLY8 |
R | PHE9 |
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 | THR180 |
R | ASN315 |
R | PHE319 |
R | HOH502 |
R | HOH508 |
R | HOH523 |
R | HOH527 |
R | HOH540 |
R | HOH552 |
R | HOH566 |
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 |