3LJP
Crystal structure of choline oxidase V464A mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| A | 0033713 | molecular_function | choline:oxygen 1-oxidoreductase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0019285 | biological_process | glycine betaine biosynthetic process from choline |
| B | 0033713 | molecular_function | choline:oxygen 1-oxidoreductase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FDA A 547 |
| Chain | Residue |
| A | GLY20 |
| A | ARG89 |
| A | ALA90 |
| A | LYS91 |
| A | VAL92 |
| A | GLY95 |
| A | CYS96 |
| A | SER97 |
| A | HIS99 |
| A | ASN100 |
| A | SER101 |
| A | GLY22 |
| A | CYS102 |
| A | ILE103 |
| A | ALA232 |
| A | SER268 |
| A | THR269 |
| A | GLY270 |
| A | ASP273 |
| A | TYR465 |
| A | ASP499 |
| A | ALA500 |
| A | SER23 |
| A | ASN510 |
| A | PRO511 |
| A | ASN512 |
| A | VAL515 |
| A | HOH554 |
| A | HOH560 |
| A | HOH563 |
| A | HOH582 |
| A | HOH583 |
| A | HOH754 |
| A | ALA24 |
| A | GLU44 |
| A | ALA45 |
| A | LEU65 |
| A | TRP71 |
| A | ALA88 |
| site_id | AC2 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE FDA B 547 |
| Chain | Residue |
| B | GLY20 |
| B | GLY22 |
| B | SER23 |
| B | ALA24 |
| B | GLU44 |
| B | ALA45 |
| B | TRP71 |
| B | ALA88 |
| B | ARG89 |
| B | ALA90 |
| B | LYS91 |
| B | VAL92 |
| B | GLY95 |
| B | CYS96 |
| B | SER97 |
| B | HIS99 |
| B | ASN100 |
| B | SER101 |
| B | CYS102 |
| B | ILE103 |
| B | LEU230 |
| B | ARG231 |
| B | ALA232 |
| B | SER268 |
| B | THR269 |
| B | GLY270 |
| B | ASP273 |
| B | TYR465 |
| B | HIS466 |
| B | ASP499 |
| B | ALA500 |
| B | ASN510 |
| B | PRO511 |
| B | ASN512 |
| B | VAL515 |
| B | HOH553 |
| B | HOH563 |
| B | HOH578 |
| B | HOH579 |
| B | HOH582 |
| B | HOH619 |
| B | HOH657 |
Functional Information from PROSITE/UniProt
| site_id | PS00624 |
| Number of Residues | 15 |
| Details | GMC_OXRED_2 GMC oxidoreductases signature 2. GAidTPkLLmlSGIG |
| Chain | Residue | Details |
| A | GLY270-GLY284 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:E4QP00 |
| Chain | Residue | Details |
| A | HIS466 | |
| B | HIS466 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER23 | |
| B | SER23 | |
| B | GLU44 | |
| B | TRP71 | |
| B | ALA90 | |
| B | CYS96 | |
| B | ALA232 | |
| B | TYR465 | |
| B | ALA500 | |
| B | ASN510 | |
| A | GLU44 | |
| A | TRP71 | |
| A | ALA90 | |
| A | CYS96 | |
| A | ALA232 | |
| A | TYR465 | |
| A | ALA500 | |
| A | ASN510 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Tele-8alpha-FAD histidine |
| Chain | Residue | Details |
| A | HIS99 | |
| B | HIS99 |
