5VMT
Crystal structure of a glyceraldehyde-3-phosphate dehydrogenase from Neisseria gonorrhoeae bound to NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 | 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 | 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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0006006 | biological_process | glucose metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| E | 0050661 | molecular_function | NADP binding |
| E | 0051287 | molecular_function | NAD binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0006006 | biological_process | glucose metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| F | 0050661 | molecular_function | NADP binding |
| F | 0051287 | molecular_function | NAD binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0006006 | biological_process | glucose metabolic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0050661 | molecular_function | NADP binding |
| G | 0051287 | molecular_function | NAD binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0006006 | biological_process | glucose metabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0050661 | molecular_function | NADP binding |
| H | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | GLY9 |
| A | GLY98 |
| A | PHE99 |
| A | PHE100 |
| A | SER120 |
| A | ALA121 |
| A | CYS151 |
| A | ASN315 |
| A | TYR319 |
| A | HOH519 |
| A | HOH529 |
| A | GLY11 |
| A | HOH534 |
| A | HOH536 |
| A | HOH541 |
| A | HOH556 |
| A | HOH573 |
| A | HOH588 |
| A | HOH603 |
| C | PRO190 |
| A | ARG12 |
| A | ILE13 |
| A | ASP34 |
| A | LEU35 |
| A | PRO78 |
| A | CYS96 |
| A | THR97 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | LYS308 |
| B | GLY230 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| B | ARG297 |
| B | LYS308 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | GLY9 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASP34 |
| B | LEU35 |
| B | PRO78 |
| B | CYS96 |
| B | THR97 |
| B | GLY98 |
| B | PHE99 |
| B | PHE100 |
| B | SER120 |
| B | ALA121 |
| B | CYS151 |
| B | ASN315 |
| B | TYR319 |
| B | HOH509 |
| B | HOH511 |
| B | HOH538 |
| B | HOH546 |
| B | HOH550 |
| B | HOH563 |
| B | HOH565 |
| B | HOH573 |
| B | HOH574 |
| B | HOH575 |
| B | HOH603 |
| D | PRO190 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue NAD C 401 |
| Chain | Residue |
| A | PRO190 |
| C | GLY9 |
| C | GLY11 |
| C | ARG12 |
| C | ILE13 |
| C | ASP34 |
| C | CYS96 |
| C | GLY98 |
| C | PHE99 |
| C | PHE100 |
| C | SER120 |
| C | ALA121 |
| C | CYS151 |
| C | ASN315 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 402 |
| Chain | Residue |
| C | ARG297 |
| C | LYS308 |
| C | HOH546 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | binding site for residue NAD D 401 |
| Chain | Residue |
| D | HOH548 |
| D | HOH562 |
| D | HOH577 |
| D | HOH579 |
| D | HOH598 |
| D | HOH602 |
| B | PRO190 |
| D | GLY9 |
| D | GLY11 |
| D | ARG12 |
| D | ILE13 |
| D | ASN33 |
| D | ASP34 |
| D | LEU35 |
| D | PRO78 |
| D | CYS96 |
| D | THR97 |
| D | GLY98 |
| D | PHE99 |
| D | SER120 |
| D | ALA121 |
| D | CYS151 |
| D | ASN315 |
| D | TYR319 |
| D | HOH506 |
| D | HOH532 |
| D | HOH539 |
| D | HOH540 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL D 402 |
| Chain | Residue |
| D | ARG297 |
| D | LYS308 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for residue NAD E 401 |
| Chain | Residue |
| E | GLY11 |
| E | ARG12 |
| E | ILE13 |
| E | ASN33 |
| E | ASP34 |
| E | LEU35 |
| E | CYS96 |
| E | GLY98 |
| E | PHE99 |
| E | PHE100 |
| E | SER120 |
| E | ALA121 |
| E | CYS151 |
| E | ASN315 |
| E | HOH532 |
| G | PRO190 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CL E 402 |
| Chain | Residue |
| E | LYS308 |
| E | HOH516 |
| F | GLY230 |
| F | SER231 |
| site_id | AD2 |
| Number of Residues | 25 |
| Details | binding site for residue NAD F 401 |
| Chain | Residue |
| F | GLY9 |
| F | GLY11 |
| F | ARG12 |
| F | ILE13 |
| F | ASP34 |
| F | LEU35 |
| F | PRO78 |
| F | CYS96 |
| F | THR97 |
| F | GLY98 |
| F | PHE99 |
| F | SER120 |
| F | ALA121 |
| F | CYS151 |
| F | ASN315 |
| F | TYR319 |
| F | HOH512 |
| F | HOH516 |
| F | HOH553 |
| F | HOH561 |
| F | HOH563 |
| F | HOH567 |
| F | HOH582 |
| H | PRO190 |
| H | HOH524 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue CL F 402 |
| Chain | Residue |
| E | GLY230 |
| F | LYS308 |
| site_id | AD4 |
| Number of Residues | 21 |
| Details | binding site for residue NAD G 401 |
| Chain | Residue |
| E | PRO190 |
| G | GLY9 |
| G | GLY11 |
| G | ARG12 |
| G | ILE13 |
| G | ASN33 |
| G | ASP34 |
| G | LEU35 |
| G | ASN77 |
| G | PRO78 |
| G | CYS96 |
| G | THR97 |
| G | GLY98 |
| G | PHE99 |
| G | PHE100 |
| G | SER120 |
| G | ALA121 |
| G | CYS151 |
| G | ASN315 |
| G | TYR319 |
| G | HOH511 |
| site_id | AD5 |
| Number of Residues | 24 |
| Details | binding site for residue NAD H 401 |
| Chain | Residue |
| F | PRO190 |
| H | GLY9 |
| H | GLY11 |
| H | ARG12 |
| H | ILE13 |
| H | ASN33 |
| H | ASP34 |
| H | LEU35 |
| H | PRO78 |
| H | CYS96 |
| H | THR97 |
| H | GLY98 |
| H | PHE99 |
| H | SER120 |
| H | ALA121 |
| H | CYS151 |
| H | ASN315 |
| H | TYR319 |
| H | HOH502 |
| H | HOH511 |
| H | HOH515 |
| H | HOH517 |
| H | HOH522 |
| H | HOH525 |
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 | ALA149-LEU156 |
