1O9B
QUINATE/SHIKIMATE DEHYDROGENASE YDIB COMPLEXED WITH NADH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
A | 0005515 | molecular_function | protein binding |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0009423 | biological_process | chorismate biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019632 | biological_process | shikimate metabolic process |
A | 0030266 | molecular_function | quinate 3-dehydrogenase (NAD+) activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0052733 | molecular_function | quinate 3-dehydrogenase (NADP+) activity |
A | 0052734 | molecular_function | shikimate 3-dehydrogenase (NAD+) activity |
B | 0004764 | molecular_function | shikimate 3-dehydrogenase (NADP+) activity |
B | 0005515 | molecular_function | protein binding |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0009423 | biological_process | chorismate biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019632 | biological_process | shikimate metabolic process |
B | 0030266 | molecular_function | quinate 3-dehydrogenase (NAD+) activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0052733 | molecular_function | quinate 3-dehydrogenase (NADP+) activity |
B | 0052734 | molecular_function | shikimate 3-dehydrogenase (NAD+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 302 |
Chain | Residue |
A | SER67 |
A | LYS71 |
A | ASP107 |
A | NAI301 |
A | HOH2088 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 303 |
Chain | Residue |
A | GLN72 |
A | MSE68 |
A | PRO69 |
A | ASN70 |
A | LYS71 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 304 |
Chain | Residue |
A | LYS32 |
A | TYR100 |
A | LYS149 |
A | GLU150 |
A | LYS152 |
A | SER196 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 B 302 |
Chain | Residue |
B | SER67 |
B | LYS71 |
B | ASP107 |
B | NAI301 |
B | HOH2065 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B 303 |
Chain | Residue |
B | MSE68 |
B | PRO69 |
B | ASN70 |
B | LYS71 |
B | GLN72 |
B | HOH2062 |
B | HOH2066 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAI A 301 |
Chain | Residue |
A | ALA132 |
A | GLY133 |
A | GLY134 |
A | ALA135 |
A | ASN155 |
A | ARG156 |
A | PHE160 |
A | GLY203 |
A | THR204 |
A | LYS205 |
A | VAL206 |
A | MSE208 |
A | CYS232 |
A | TYR234 |
A | GLY255 |
A | MSE258 |
A | LEU259 |
A | PO4302 |
A | HOH2058 |
site_id | AC7 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAI B 301 |
Chain | Residue |
B | ASP107 |
B | ALA132 |
B | GLY133 |
B | GLY134 |
B | ALA135 |
B | ASN155 |
B | ARG156 |
B | ASP158 |
B | PHE160 |
B | GLY203 |
B | THR204 |
B | LYS205 |
B | VAL206 |
B | MSE208 |
B | CYS232 |
B | VAL233 |
B | TYR234 |
B | GLY255 |
B | MSE258 |
B | LEU259 |
B | PO4302 |
B | HOH2044 |
B | HOH2062 |
B | HOH2063 |
B | HOH2064 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01578 |
Chain | Residue | Details |
A | LYS71 | |
A | ASP107 | |
B | LYS71 | |
B | ASP107 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01578, ECO:0000269|PubMed:12624088, ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:16021622 |
Chain | Residue | Details |
A | ALA132 | |
B | GLY255 | |
A | ASN155 | |
A | LYS205 | |
A | CYS232 | |
A | GLY255 | |
B | ALA132 | |
B | ASN155 | |
B | LYS205 | |
B | CYS232 |