3M6I
L-arabinitol 4-dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003939 | molecular_function | L-iditol 2-dehydrogenase activity |
A | 0006062 | biological_process | sorbitol catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0019568 | biological_process | arabinose catabolic process |
A | 0019569 | biological_process | L-arabinose catabolic process to xylulose 5-phosphate |
A | 0046872 | molecular_function | metal ion binding |
A | 0050019 | molecular_function | L-arabinitol 4-dehydrogenase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003939 | molecular_function | L-iditol 2-dehydrogenase activity |
B | 0006062 | biological_process | sorbitol catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0019568 | biological_process | arabinose catabolic process |
B | 0019569 | biological_process | L-arabinose catabolic process to xylulose 5-phosphate |
B | 0046872 | molecular_function | metal ion binding |
B | 0050019 | molecular_function | L-arabinitol 4-dehydrogenase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | CYS53 |
A | HIS78 |
A | GLU79 |
A | HOH412 |
A | NAD501 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 402 |
Chain | Residue |
A | CYS108 |
A | CYS111 |
A | CYS114 |
A | CYS122 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NAD A 501 |
Chain | Residue |
A | GLY54 |
A | SER55 |
A | VAL167 |
A | GLY189 |
A | PRO190 |
A | ILE191 |
A | ASP211 |
A | ILE212 |
A | ARG216 |
A | CYS259 |
A | THR260 |
A | ILE282 |
A | GLY283 |
A | VAL284 |
A | GLN306 |
A | ARG308 |
A | HOH377 |
A | ZN401 |
A | HOH421 |
A | HOH441 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 401 |
Chain | Residue |
B | CYS53 |
B | HIS78 |
B | GLU79 |
B | GLU163 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 402 |
Chain | Residue |
B | CYS108 |
B | CYS111 |
B | CYS114 |
B | CYS122 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NAD B 501 |
Chain | Residue |
B | VAL167 |
B | GLY189 |
B | PRO190 |
B | ILE191 |
B | THR210 |
B | ASP211 |
B | ILE212 |
B | ARG216 |
B | VAL232 |
B | CYS259 |
B | THR260 |
B | ILE282 |
B | VAL284 |
B | GLN306 |
B | ARG308 |
B | HOH367 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 26 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20655316 |
Chain | Residue | Details |
A | CYS111 | |
A | CYS114 | |
A | CYS122 | |
A | GLU163 | |
A | PRO190 | |
A | ASP211 | |
A | ARG216 | |
A | ILE282 | |
A | GLN306 | |
B | CYS53 | |
B | HIS78 | |
B | GLU79 | |
B | CYS108 | |
B | CYS111 | |
B | CYS114 | |
B | CYS122 | |
B | GLU163 | |
B | PRO190 | |
B | ASP211 | |
B | ARG216 | |
B | ILE282 | |
B | GLN306 | |
A | CYS53 | |
A | HIS78 | |
A | GLU79 | |
A | CYS108 |