6F97
Crystal structure of the V465T mutant of 5-(Hydroxymethyl)furfural Oxidase (HMFO)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008812 | molecular_function | choline dehydrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0016670 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor |
| A | 0016899 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0055114 | biological_process | obsolete oxidation-reduction process |
| A | 0071949 | molecular_function | FAD binding |
| B | 0008812 | molecular_function | choline dehydrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0016670 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor |
| B | 0016899 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0055114 | biological_process | obsolete oxidation-reduction process |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 39 |
| Details | binding site for residue FAD A 700 |
| Chain | Residue |
| A | GLY12 |
| A | GLY92 |
| A | ARG93 |
| A | LEU94 |
| A | GLY97 |
| A | GLY98 |
| A | VAL101 |
| A | ASN102 |
| A | MET103 |
| A | VAL104 |
| A | VAL105 |
| A | GLY14 |
| A | SER231 |
| A | VAL233 |
| A | THR265 |
| A | ALA266 |
| A | GLY267 |
| A | GLN270 |
| A | TRP466 |
| A | ASP500 |
| A | ALA501 |
| A | ASN511 |
| A | THR15 |
| A | THR512 |
| A | ASN513 |
| A | THR516 |
| A | HOH815 |
| A | HOH822 |
| A | HOH826 |
| A | HOH861 |
| A | HOH873 |
| A | HOH880 |
| A | HOH887 |
| A | ALA16 |
| A | ILE35 |
| A | GLU36 |
| A | ALA37 |
| A | TRP68 |
| A | GLU90 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | binding site for residue FAD B 700 |
| Chain | Residue |
| B | GLY12 |
| B | GLY14 |
| B | THR15 |
| B | ALA16 |
| B | ILE35 |
| B | GLU36 |
| B | ALA37 |
| B | TRP68 |
| B | GLU90 |
| B | GLY92 |
| B | ARG93 |
| B | LEU94 |
| B | GLY98 |
| B | VAL104 |
| B | VAL105 |
| B | SER231 |
| B | VAL233 |
| B | THR265 |
| B | ALA266 |
| B | TRP466 |
| B | ASP500 |
| B | ALA501 |
| B | ASN511 |
| B | THR512 |
| B | ASN513 |
| B | THR516 |
| B | HOH807 |
| B | HOH836 |
| B | HOH844 |
| B | HOH850 |
| B | HOH858 |
| B | HOH859 |
| B | HOH887 |
| B | HOH897 |
| B | HOH912 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:24271187, ECO:0000305|DOI:10.1021/ACSCATAL.5B00031 |
| Chain | Residue | Details |
| A | HIS467 | |
| B | HIS467 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000305|DOI:10.1021/ACSCATAL.5B00031, ECO:0007744|PDB:4UDP, ECO:0007744|PDB:4UDQ, ECO:0007744|PDB:4UDR |
| Chain | Residue | Details |
| A | THR15 | |
| B | THR15 | |
| B | GLU36 | |
| B | TRP68 | |
| B | LEU94 | |
| B | GLY98 | |
| B | ASN102 | |
| B | VAL233 | |
| B | ALA501 | |
| B | THR512 | |
| A | GLU36 | |
| A | TRP68 | |
| A | LEU94 | |
| A | GLY98 | |
| A | ASN102 | |
| A | VAL233 | |
| A | ALA501 | |
| A | THR512 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:4UDR |
| Chain | Residue | Details |
| A | TRP466 | |
| B | TRP466 |
