4MJW
Crystal Structure of Choline Oxidase in Complex with the Reaction Product Glycine Betaine
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 | 44 |
| Details | BINDING SITE FOR RESIDUE FAD A 601 |
| Chain | Residue |
| A | GLY20 |
| A | ALA90 |
| A | LYS91 |
| A | VAL92 |
| A | GLY95 |
| A | CYS96 |
| A | SER97 |
| A | HIS99 |
| A | ASN100 |
| A | SER101 |
| A | CYS102 |
| A | GLY22 |
| A | ILE103 |
| A | LEU230 |
| A | ARG231 |
| A | ALA232 |
| A | SER268 |
| A | THR269 |
| A | GLY270 |
| A | ASP273 |
| A | LEU277 |
| A | TYR465 |
| A | SER23 |
| A | HIS466 |
| A | ASP499 |
| A | ALA500 |
| A | ASN510 |
| A | PRO511 |
| A | ASN512 |
| A | VAL515 |
| A | BET602 |
| A | HOH706 |
| A | HOH711 |
| A | ALA24 |
| A | HOH786 |
| A | HOH789 |
| A | HOH790 |
| A | HOH791 |
| A | HOH922 |
| A | GLU44 |
| A | ALA45 |
| A | TRP71 |
| A | ALA88 |
| A | ARG89 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BET A 602 |
| Chain | Residue |
| A | SER101 |
| A | HIS351 |
| A | VAL464 |
| A | HIS466 |
| A | ASN510 |
| A | FAD601 |
| A | HOH927 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 603 |
| Chain | Residue |
| A | ARG363 |
| B | SER392 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 604 |
| Chain | Residue |
| A | VAL298 |
| A | ASP299 |
| A | PRO301 |
| A | GLU479 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 605 |
| Chain | Residue |
| A | ARG391 |
| site_id | AC6 |
| Number of Residues | 42 |
| Details | BINDING SITE FOR RESIDUE FAD B 601 |
| Chain | Residue |
| B | HOH805 |
| 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 | BET602 |
| B | HOH711 |
| B | HOH794 |
| B | HOH800 |
| B | HOH801 |
| B | HOH802 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BET B 602 |
| Chain | Residue |
| B | SER101 |
| B | TRP331 |
| B | HIS351 |
| B | VAL464 |
| B | HIS466 |
| B | ASN510 |
| B | FAD601 |
| B | HOH947 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT B 603 |
| Chain | Residue |
| A | SER392 |
| B | ARG363 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 604 |
| Chain | Residue |
| B | VAL298 |
| B | ASP299 |
| B | PRO301 |
| B | GLU479 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 605 |
| Chain | Residue |
| A | PHE84 |
| B | ARG391 |
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 |
