Brand  (β version)

PDB ID: 1MXT

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
FAE Flavin-n7 protonated-adenine dinucleotide PoSSuM
OXY Oxygen molecule PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1MXT   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Atomic resolution structure of Cholesterol oxidase (Streptomyces sp. SA-COO)
Release Data : 2003-02-25
Compound :
mol_id molecule chains synonym
1 CHOLESTEROL OXIDASE A CHOD
ec: 1.1.3.6
other_details: FAD COFACTOR NON-COVALENTLY BOUND TO THE ENZYME
Source :
mol_id organism_scientific expression_system
1 Streptomyces sp.  (taxid:1931) Escherichia coli  (taxid:562)
gene: CHOA
expression_system_strain: BL21(DE3)PLYSS
expression_system_vector_type: PLASMID
expression_system_plasmid: PCO202
Authors : Vrielink, A., Lario, P.I.
Keywords : FLAVOENZYME, STEROID METABOLISM, OXIDOREDUCTASE, ATOMIC RESOLUTION
Exp. method : X-RAY DIFFRACTION ( 0.95 Å )
Citation :

Sub-atomic resolution crystal structure of cholesterol oxidase: What atomic resolution crystallography reveals about enzyme mechanism and the role of FAD cofactor in redox activity

Lario, P.I.,Sampson, N.,Vrielink, A.
(2003)  J.Mol.Biol.  326 : 1635 - 1650

PubMed: 12595270
DOI: 10.1016/S0022-2836(03)00054-8

Atomic resolution crystallography reveals how changes in pH shape the protein microenvironment

Lyubimov, A.Y.,Lario, P.I.,Moustafa, I.  et al.
(2006)  Nat.Chem.Biol.  2 : 259 - 264

PubMed: 16604066
DOI: 10.1038/nchembio784

Reaction

Chain : A
UniProt : P12676 (CHOD_STRS0)
Reaction: EC: Evidence:
Physiological Direction:
cholesterol + O2 = cholest-5-en-3-one + H2O2 1.1.3.6 PubMed:9922167
left-to-right
cholest-5-en-3-one = cholest-4-en-3-one 5.3.3.1 PubMed:9922167
left-to-right