6IQM
Crystal Structure of Cell Surface Glyceraldehyde-3-Phosphate Dehydrogenase Complexed with NAD+ from Lactobacillus plantarum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006006 | biological_process | glucose metabolic process |
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 | 0006006 | biological_process | glucose metabolic process |
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 | 0006006 | biological_process | glucose metabolic process |
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 | 0006006 | biological_process | glucose metabolic process |
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 | 33 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | ASN8 |
A | GLU81 |
A | PRO82 |
A | CYS101 |
A | THR102 |
A | GLY103 |
A | PHE104 |
A | SER125 |
A | ALA126 |
A | GLU323 |
A | PHE326 |
A | GLY9 |
A | HOH505 |
A | HOH509 |
A | HOH513 |
A | HOH522 |
A | HOH533 |
A | HOH541 |
A | HOH555 |
A | HOH581 |
A | HOH680 |
A | HOH691 |
A | PHE10 |
A | HOH700 |
A | HOH718 |
A | HOH745 |
A | HOH751 |
A | GLY11 |
A | ARG12 |
A | ILE13 |
A | ASN37 |
A | ASP38 |
A | LEU39 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | HIS47 |
A | VAL62 |
A | HOH558 |
A | HOH577 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | ARG12 |
A | ARG15 |
A | ARG19 |
A | LEU48 |
A | LEU49 |
A | ASP52 |
A | HOH607 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue TRS B 401 |
Chain | Residue |
A | GLY208 |
A | GLY241 |
A | HOH545 |
A | HOH593 |
B | GLY208 |
B | GLY241 |
B | HOH518 |
B | HOH744 |
C | HOH540 |
C | HOH583 |
D | GLY208 |
D | GLY241 |
D | HOH530 |
D | HOH570 |
site_id | AC5 |
Number of Residues | 31 |
Details | binding site for residue NAD B 402 |
Chain | Residue |
B | ASN8 |
B | GLY9 |
B | GLY11 |
B | ARG12 |
B | ILE13 |
B | ASN37 |
B | ASP38 |
B | PRO82 |
B | CYS101 |
B | THR102 |
B | GLY103 |
B | SER125 |
B | ALA126 |
B | CYS156 |
B | SER187 |
B | ASN322 |
B | PHE326 |
B | HOH510 |
B | HOH514 |
B | HOH522 |
B | HOH530 |
B | HOH537 |
B | HOH569 |
B | HOH605 |
B | HOH639 |
B | HOH670 |
B | HOH675 |
B | HOH679 |
B | HOH718 |
D | PRO195 |
D | HOH631 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | HIS47 |
B | VAL62 |
B | HOH534 |
B | HOH600 |
B | HOH602 |
site_id | AC7 |
Number of Residues | 32 |
Details | binding site for residue NAD C 401 |
Chain | Residue |
C | ARG12 |
C | ILE13 |
C | ASN37 |
C | ASP38 |
C | PRO82 |
C | CYS101 |
C | THR102 |
C | GLY103 |
C | PHE104 |
C | SER125 |
C | ALA126 |
C | CYS156 |
C | SER187 |
C | ASN322 |
C | PHE326 |
C | HOH531 |
C | HOH532 |
C | HOH551 |
C | HOH584 |
C | HOH594 |
C | HOH595 |
C | HOH614 |
C | HOH625 |
C | HOH637 |
C | HOH661 |
C | HOH672 |
C | HOH684 |
A | PRO195 |
A | HOH634 |
C | ASN8 |
C | GLY9 |
C | GLY11 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO C 402 |
Chain | Residue |
C | HIS47 |
C | VAL62 |
C | HOH582 |
C | HOH597 |
C | HOH598 |
site_id | AC9 |
Number of Residues | 32 |
Details | binding site for residue NAD D 401 |
Chain | Residue |
B | PRO195 |
B | HOH624 |
D | ASN8 |
D | GLY9 |
D | PHE10 |
D | GLY11 |
D | ARG12 |
D | ILE13 |
D | ASN37 |
D | ASP38 |
D | PRO82 |
D | CYS101 |
D | THR102 |
D | GLY103 |
D | PHE104 |
D | SER125 |
D | ALA126 |
D | CYS156 |
D | ASN322 |
D | PHE326 |
D | HOH528 |
D | HOH549 |
D | HOH566 |
D | HOH573 |
D | HOH600 |
D | HOH611 |
D | HOH627 |
D | HOH635 |
D | HOH655 |
D | HOH688 |
D | HOH700 |
D | HOH739 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO D 402 |
Chain | Residue |
D | HIS47 |
D | VAL62 |
D | HOH551 |
D | HOH601 |
D | HOH623 |