6GHL
cyanobacterial GAPDH with full-length CP12
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 | 0046872 | molecular_function | metal ion binding |
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 | 0046872 | molecular_function | metal ion binding |
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 | 0046872 | molecular_function | metal ion binding |
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 | 0046872 | molecular_function | metal ion binding |
D | 0050661 | molecular_function | NADP binding |
D | 0051287 | molecular_function | NAD binding |
E | 0080153 | biological_process | negative regulation of reductive pentose-phosphate cycle |
F | 0080153 | biological_process | negative regulation of reductive pentose-phosphate cycle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | binding site for residue NAD A 1001 |
Chain | Residue |
A | GLY8 |
A | THR100 |
A | GLY101 |
A | THR123 |
A | ALA124 |
A | CYS154 |
A | ASN317 |
A | TYR321 |
A | HOH1107 |
A | HOH1117 |
A | HOH1119 |
A | PHE9 |
A | HOH1129 |
D | HOH1117 |
E | GLU69 |
F | HIS45 |
A | GLY10 |
A | ARG11 |
A | ILE12 |
A | ASP36 |
A | THR37 |
A | ARG81 |
A | ALA99 |
site_id | AC2 |
Number of Residues | 26 |
Details | binding site for residue NAD B 1001 |
Chain | Residue |
B | GLY8 |
B | PHE9 |
B | GLY10 |
B | ARG11 |
B | ILE12 |
B | ASN35 |
B | ASP36 |
B | THR37 |
B | ASP80 |
B | ARG81 |
B | ALA99 |
B | THR100 |
B | GLY101 |
B | THR123 |
B | ALA124 |
B | CYS154 |
B | THR184 |
B | ASN317 |
B | GLU318 |
B | TYR321 |
B | HOH1112 |
B | HOH1118 |
B | HOH1120 |
C | HOH1110 |
F | ASP66 |
F | TYR73 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue NAD C 1001 |
Chain | Residue |
C | GLY8 |
C | PHE9 |
C | GLY10 |
C | ARG11 |
C | ILE12 |
C | ASN35 |
C | ASP36 |
C | THR37 |
C | ARG81 |
C | ALA99 |
C | THR100 |
C | GLY101 |
C | THR123 |
C | ALA124 |
C | CYS154 |
C | ASN317 |
C | TYR321 |
C | HOH1129 |
C | HOH1130 |
C | HOH1138 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue MLI C 1002 |
Chain | Residue |
C | SER153 |
C | CYS154 |
C | THR155 |
C | ARG199 |
C | THR212 |
C | GLY213 |
C | ARG235 |
C | HOH1141 |
site_id | AC5 |
Number of Residues | 23 |
Details | binding site for residue NAD D 1001 |
Chain | Residue |
E | TYR73 |
D | GLY8 |
D | PHE9 |
D | GLY10 |
D | ARG11 |
D | ILE12 |
D | ASN35 |
D | ASP36 |
D | THR37 |
D | ARG81 |
D | ALA99 |
D | GLY101 |
D | THR123 |
D | ALA124 |
D | CYS154 |
D | THR184 |
D | ASN317 |
D | TYR321 |
D | HOH1102 |
D | HOH1106 |
D | HOH1110 |
D | HOH1111 |
E | ASP66 |
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 | ALA152-LEU159 |