5LD5
Crystal structure of a bacterial dehydrogenase at 2.19 Angstroms resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
A | 0006006 | biological_process | glucose metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
A | 0050661 | molecular_function | NADP binding |
A | 0051287 | molecular_function | NAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
B | 0006006 | biological_process | glucose metabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
B | 0050661 | molecular_function | NADP binding |
B | 0051287 | molecular_function | NAD binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
C | 0006006 | biological_process | glucose metabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
C | 0050661 | molecular_function | NADP binding |
C | 0051287 | molecular_function | NAD binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
D | 0006006 | biological_process | glucose metabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | GLY24 |
A | GLY115 |
A | PHE116 |
A | SER137 |
A | ALA138 |
A | ASN336 |
A | TYR340 |
A | HOH508 |
A | HOH517 |
A | HOH529 |
A | HOH538 |
A | GLY26 |
A | HOH544 |
A | HOH547 |
B | PRO207 |
B | HOH520 |
A | ARG27 |
A | ILE28 |
A | ASP49 |
A | LEU50 |
A | ALA95 |
A | CYS113 |
A | THR114 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 402 |
Chain | Residue |
A | ASN68 |
A | ARG71 |
A | HOH513 |
D | ASP301 |
D | TYR307 |
D | HOH536 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | ASN68 |
A | TYR69 |
A | ASN72 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | PRO139 |
A | SER167 |
A | THR228 |
A | GLY229 |
A | ALA230 |
A | HOH501 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | ALA220 |
A | PRO253 |
B | PRO253 |
C | ALA220 |
D | ALA220 |
site_id | AC6 |
Number of Residues | 22 |
Details | binding site for residue NAD B 401 |
Chain | Residue |
A | PRO207 |
A | HOH510 |
B | GLY24 |
B | GLY26 |
B | ARG27 |
B | ILE28 |
B | ASP49 |
B | LEU50 |
B | ALA95 |
B | CYS113 |
B | THR114 |
B | GLY115 |
B | SER137 |
B | ALA138 |
B | CYS168 |
B | ASN336 |
B | TYR340 |
B | HOH509 |
B | HOH511 |
B | HOH526 |
B | HOH528 |
B | HOH543 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | ASP301 |
B | MET305 |
B | TYR307 |
C | ASN68 |
C | ARG71 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | THR314 |
D | ARG214 |
D | ASN226 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | ASN150 |
B | VAL151 |
B | HIS153 |
B | GLU154 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue GOL B 405 |
Chain | Residue |
B | TYR62 |
B | ASN68 |
B | ARG71 |
C | ASP301 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue GOL B 406 |
Chain | Residue |
B | ARG214 |
B | HOH544 |
D | THR314 |
site_id | AD3 |
Number of Residues | 25 |
Details | binding site for residue NAD C 401 |
Chain | Residue |
C | TYR340 |
C | HOH511 |
C | HOH516 |
C | HOH530 |
C | HOH532 |
C | HOH540 |
C | HOH546 |
C | HOH549 |
C | HOH551 |
D | PRO207 |
C | GLY24 |
C | GLY26 |
C | ARG27 |
C | ILE28 |
C | ASN48 |
C | ASP49 |
C | LEU50 |
C | ALA95 |
C | CYS113 |
C | THR114 |
C | GLY115 |
C | PHE116 |
C | SER137 |
C | ALA138 |
C | ASN336 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue GOL C 402 |
Chain | Residue |
A | THR314 |
A | HOH553 |
C | ARG214 |
C | ASN226 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue GOL C 403 |
Chain | Residue |
C | VAL274 |
C | ASN278 |
C | ALA313 |
C | THR314 |
C | THR316 |
site_id | AD6 |
Number of Residues | 26 |
Details | binding site for residue NAD D 401 |
Chain | Residue |
C | PRO207 |
C | HOH536 |
D | GLY24 |
D | GLY26 |
D | ARG27 |
D | ILE28 |
D | ASN48 |
D | ASP49 |
D | LEU50 |
D | ALA95 |
D | CYS113 |
D | THR114 |
D | GLY115 |
D | PHE116 |
D | SER137 |
D | ALA138 |
D | ASN336 |
D | TYR340 |
D | HOH515 |
D | HOH517 |
D | HOH531 |
D | HOH535 |
D | HOH538 |
D | HOH541 |
D | HOH547 |
D | HOH548 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue GOL D 402 |
Chain | Residue |
D | ASN68 |
D | ARG71 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
A | ALA166-LEU173 |
site_id | PS00430 |
Number of Residues | 89 |
Details | TONB_DEPENDENT_REC_1 TonB-dependent receptor (TBDR) proteins signature 1. gamkedrlpanlakgesmavkvaingfgrigrlafrqmfghegseivaindltdpkmlanllkydssqgnyarnhsvvage..................................DSITVDGK |
Chain | Residue | Details |
A | GLY-1-LYS87 |