Structure of PDB 2xlp Chain D

Receptor sequence

>2xlpD (length=446) Species: 230105 (Methylophaga aminisulfidivorans) [Search protein sequence]

ATRIAILGAGPSGMAQLRAFQSAQEKGAEIPELVCFEKQADWGGQWNYTW
RTGLDENGEPVHSSMYRYLWSSGPKECLEFADYTFDEHFGKPIASYPPRE
VLWDYIKGRVEKAGVRKYIRFNTAVRHVEFNEDSQTFTVTVQDHTTDTIY
SAAFDYVVCCTGHFSTPYVPEFEGFEKFGGRILHAHDFRDALEFKDKTVL
LVGSSYSAEDIGSQCYKYGAKKLISCYRTAPMGYKWPENWDERPNLVRVD
TENAYFADGSSEKVDAIILCTGYIHHFPFLNDDLRLVTNNRLWPLNLYKG
VVWEDNPKFFYIGMQDQWYSFNMFDAQAWYARDVIMGRLPLPSKEEMKAD
SMAWREKELTLVTAEEMYTYQGDYIQNLIDMTDYPSFDIPATNKTFLEWK
HHKKENIMTFRDHSYRSLMTGTMAPKHHTPWIDALDDSLEAYLSDK

3D structure

PDB

2xlp Joint functions of protein residues and NADP(H) in oxygen activation by flavin-containing monooxygenase.

Chain

Resolution

2.8 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	D	G14 G16 P17 S18 E43 K44 Q45 G50 Q51 W52 H68 S70 M71 S77 A130 V131 C166 T167 F170 Q323 S326 F330	G8 G10 P11 S12 E37 K38 Q39 G44 Q45 W46 H62 S64 M65 S71 A124 V125 C160 T161 F164 Q317 S320 F324
BS02	NAP	D	L75 S78 F170 S210 S211 Y212 S213 D216 R234 C276 T277	L69 S72 F164 S204 S205 Y206 S207 D210 R228 C270 T271

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:2xlp, PDBe:2xlp, PDBj:2xlp
PDBsum	2xlp
PubMed	20807767
UniProt	Q83XK4

[Back to BioLiP]