Structure of PDB 2xls Chain B

Receptor sequence

>2xlsB (length=447) Species: 230105 (Methylophaga aminisulfidivorans) [Search protein sequence]

MATRIAILGAGPSGMAQLRAFQSAQEKGAEIPELVCFEKQADWGGQWNYT
WRTGLDENGEPVHSSMYRYLWSKGPKECLEFADYTFDEHFGKPIASYPPR
EVLWDYIKGRVEKAGVRKYIRFNTAVRHVEFNEDSQTFTVTVQDHTTDTI
YSAAFDYVVCCTGHFSTPYVPEFEGFEKFGGRILHAHDFRDALEFKDKTV
LLVGSSYSAEDIGSQCYKYGAKKLISCYRTAPMGYKWPENWDERPNLVRV
DTENAYFADGSSEKVDAIILCTGYIHHFPFLNDDLRLVTNNRLWPLNLYK
GVVWEDNPKFFYIGMQDQWYSFNMFDAQAWYARDVIMGRLPLPSKEEMKA
DSMAWREKELTLVTAEEMYTYQGDYIQNLIDMTDYPSFDIPATNKTFLEW
KHHKKENIMTFRDHSYRSLMTGTMAPKHHTPWIDALDDSLEAYLSDK

3D structure

PDB

2xls Joint-Functions of Protein Residues and Nadp(H) in Oxygen-Activation by Flavin-Containing Monooxygenase

Chain

Resolution

3.0 Å

3D
structure

[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Enzyme Commision number

1.14.13.148: trimethylamine monooxygenase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FAD	B	G14 G16 P17 S18 E43 K44 Q45 G50 Q51 W52 H68 M71 S77 K78 A130 V131 C166 T167 F170 Q323 S326 F330	G9 G11 P12 S13 E38 K39 Q40 G45 Q46 W47 H63 M66 S72 K73 A125 V126 C161 T162 F165 Q318 S321 F325
BS02	NAP	B	K78 F170 S210 S211 Y212 S213 R234 T235 N251 C276 T277 G278	K73 F165 S205 S206 Y207 S208 R229 T230 N246 C271 T272 G273

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0004497	monooxygenase activity
GO:0004499	N,N-dimethylaniline monooxygenase activity
GO:0042802	identical protein binding
GO:0050660	flavin adenine dinucleotide binding
GO:0050661	NADP binding

View graph for
Molecular Function

External links

PDB	RCSB:2xls, PDBe:2xls, PDBj:2xls
PDBsum	2xls
PubMed	20807767
UniProt	Q83XK4

[Back to BioLiP]