Brand  (β version)

color scheme of protein:


interaction residue:

chain: Hide other chain(s)

Code Name Link
1PE Pentaethylene glycol
ACT Acetate ion
CA Calcium ion
HEC Heme C
PG4 Tetraethylene glycol
Modified Residues
Code Name Link
0AF 7-hydroxy-L-tryptophan
Code : 3L4M
Title : Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex.
Release Data : 2010-03-23
Compound :
mol_id molecule chains
1 Methylamine utilization protein mauG A,B
ec: 1.-.-.-
mol_id molecule chains synonym
2 Methylamine dehydrogenase light chain C,E MADH
fragment: Beta chain of immature methylamine dehydrogenase (preMADH)
mutation: Trp57 is hydroxylated at C7
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:318586)
strain: Pd 1222
gene: mauG
mol_id organism_scientific expression_system
2 Paracoccus denitrificans  (taxid:318586) Rhodobacter sphaeroides  (taxid:1063)
strain: Pd 1222
gene: mauA
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, quinone cofactor, TTQ, His-Tyr heme, Electron transport, c-heme, Iron, Metal-binding, Oxidoreductase, Transport, Disulfide bond, OXIDOREDUCTASE-ELECTRON TRANSPORT complex
Exp. method : X-RAY DIFFRACTION ( 2.020 Å )
Citation :

In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex.

Jensen, L.M.,Sanishvili, R.,Davidson, V.L.  et al.
(2010)  Science  327 : 1392 - 1394

PubMed: 20223990
DOI: 10.1126/science.1182492

Chain : A, B
UniProt : Q51658 (MAUG_PARDP)
Reaction : -
Chain : C, E
UniProt : P22619 (DHML_PARDE)
Reaction : Methylamine + H(2)O + 2 oxidized [amicyanin] = formaldehyde + NH(3) + 2 reduced [amicyanin].
Chain : D, F
UniProt : A1BB97 (No found in current UniProtKB/SwissProt)
Reaction : -