Brand  (β version)

  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
FDA Dihydroflavine-adenine dinucleotide
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1TVC   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)
Release Data : 2004-10-12
Compound :
mol_id molecule chains synonym
1 METHANE MONOOXYGENASE COMPONENT C A Methane hydroxylase; Methane monooxygenase reductase; MMOR
ec: 1.14.13.25
fragment: C-TERMINAL DOMAIN
Source :
mol_id organism_scientific expression_system
1 Methylococcus capsulatus  (taxid:414) Escherichia coli BL21(DE3)  (taxid:469008)
gene: mmoC
expression_system_strain: BL21(DE3)
expression_system_vector_type: PLASMID
expression_system_plasmid: pFAD21
Authors : Chatwood, L.L., Mueller, J., Gross, J.D., Wagner, G., Lippard, S.J.
Keywords : FAD-BINDING; NADH-BINDING, OXIDOREDUCTASE
Exp. method : SOLUTION NMR
Citation :

NMR Structure of the Flavin Domain from Soluble Methane Monooxygenase Reductase from Methylococcus capsulatus (Bath)

Chatwood, L.L.,Gross, J.D.,Wagner, G.  et al.
(2004)  Biochemistry  43 : 11983 - 11991

PubMed: 15379538
DOI: 10.1021/bi049066n

Chain : A
UniProt : P22868 (MMOC_METCA)
Reaction: EC: Evidence:
Physiological Direction:
H(+) + methane + NADH + O2 = H2O + methanol + NAD(+) 1.14.13.25 -
-
H(+) + methane + NADPH + O2 = H2O + methanol + NADP(+) 1.14.13.25 -
-