Brand  (β version)

color scheme of protein:


interaction residue:

chain: Hide other chain(s)

Code Name Link
ACT Acetate ion
CA Calcium ion
EDO 1,2-ethanediol
HEC Heme C
MES 2-(N-morpholino)-ethanesulfonic acid
NA Sodium ion
P6G Hexaethylene glycol
PEG Di(hydroxyethyl)ether
PG4 Tetraethylene glycol
Modified Residues
Code Name Link
0AF 7-hydroxy-L-tryptophan
Code : 3RMZ
Header : Oxidoreductase/electron transport
Title : Crystal Structure of the W199F-MauG/pre-Methylamine Dehydrogenase Complex
Release Data : 2011-10-05
Compound :
mol_id molecule chains
1 Methylamine utilization protein MauG A,B
ec: 1.-.-.-
mutation: W199F
mol_id molecule chains
2 Methylamine dehydrogenase light chain C,E
mol_id molecule chains
3 Methylamine dehydrogenase heavy chain D,F
Source :
mol_id organism_scientific expression_system
1 Paracoccus denitrificans  (taxid:318586) Paracoccus denitrificans  (taxid:266)
strain: Pd 1222
gene: mauG, Pden_4736
mol_id organism_scientific expression_system
2 Paracoccus denitrificans  (taxid:318586) Rhodobacter sphaeroides  (taxid:1063)
strain: Pd 1222
gene: Pden_4733
mol_id organism_scientific expression_system
3 Paracoccus denitrificans  (taxid:318586) Rhodobacter sphaeroides  (taxid:1063)
strain: Pd 1222
gene: Pden_4730
Authors : Jensen, L.M.R., Wilmot, C.M.
Keywords : MauG, methylamine dehydrogenase, c-heme, quinone cofactor, ELECTRON TRANSPORT, Oxidoreductase-electron transport complex
Exp. method : X-RAY DIFFRACTION ( 1.72 Å )
Citation :

Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis.

Tarboush, N.A.,Jensen, L.M.,Yukl, E.T.  et al.
(2011)  Proc.Natl.Acad.Sci.USA  108 : 16956 - 16961

PubMed: 21969534
DOI: 10.1073/pnas.1109423108

Chain : A, B
UniProt : Q51658 (MAUG_PARDP)
Reaction : -
Chain : C, E
UniProt : A1BBA0 (No found in current UniProtKB/SwissProt)
Reaction : -
Chain : D, F
UniProt : A1BB97 (No found in current UniProtKB/SwissProt)
Reaction : -