Structure of PDB 1djq Chain B

Receptor sequence

>1djqB (length=729) Species: 2327 (Methylophilus methylotrophus W3A1) [Search protein sequence]

ARDPKHDILFEPIQIGPKTLRNRFYQVPHAIGAGSDKPGFQSAHRSVKAE
GGWAALNTEYCSINPESDDTHRLSARIWDEGDVRNLKAMTDEVHKYGALA
GVELWYGGAHAPNMESRATPRGPSQYASEFETLSYCKEMDLSDIAQVQQF
YVDAAKRSRDAGFDIVYVYGAHSYLPLQFLNPYYNKRTDKYGGSLENRAR
FWLETLEKVKHAVGSDCAIATRFGVDTVYGPGQIEAEVDGQKFVEMADSL
VDMWDITIGDIAEWGEDAGPSRFYQQGHTIPWVKLVKQVSKKPVLGVGRY
TDPEKMIEIVTKGYADIIGCARPSIADPFLPQKVEQGRYDDIRVCIGCNV
CISRWEIGGPPMICTQNATAGEEYRRGWHPEKFRQTKNKDSVLIVGAGPS
GSEAARVLMESGYTVHLTDTAEKIGGHLNQVAALPGLGEWSYHRDYRETQ
ITKLLKKNKESQLALGQKPMTADDVLQYGADKVIIATGARWNTDGTNCLT
HDPIPGADASLPDQLTPEQVMDGKKKIGKRVVILNADTYFMAPSLAEKLA
TAGHEVTIVSGVHLANYMHFTLEYPNMMRRLHELHVEELGDHFCSRIEPG
RMEIYNIWGDGSKRTYRGPGVSPRDANTSHRWIEFDSLVLVTGRHSECTL
WNELKARESEWAENDIKGIYLIGDAEAPRLIADATFTGHRVAREIEEANP
QIAIPYKRETIAWGTPHMPGGNFKIEYKV

3D structure

PDB

1djq Structural and biochemical characterization of recombinant wild type and a C30A mutant of trimethylamine dehydrogenase from methylophilus methylotrophus (sp. W(3)A(1)).

Chain

Resolution

2.2 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	A30 Y169 H172 Y174 R222 Y229 D267 V350
Catalytic site (residue number reindexed from 1)	A30 Y169 H172 Y174 R222 Y229 D267 V350
Enzyme Commision number	1.5.8.2: trimethylamine dehydrogenase.

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)
BS01	SF4	B	R322 I325 C345 I346 G347 C348 N349 C351 C364 T365	R322 I325 C345 I346 G347 C348 N349 C351 C364 T365
BS02	FMN	B	P28 H29 A30 E59 Y60 E103 Y169 R222 W264 D267 A268 V297 R299 C320 A321 R322 P323 I352	P28 H29 A30 E59 Y60 E103 Y169 R222 W264 D267 A268 V297 R299 C320 A321 R322 P323 I352
BS03	ADP	B	V395 G396 G398 P399 S400 D419 G426 H427 M470 T487 G488 D674	V395 G396 G398 P399 S400 D419 G426 H427 M470 T487 G488 D674

Gene Ontology

	Molecular Function
GO:0010181	FMN binding
GO:0016491	oxidoreductase activity
GO:0046872	metal ion binding
GO:0050470	trimethylamine dehydrogenase activity
GO:0051539	4 iron, 4 sulfur cluster binding

	Biological Process
GO:0009056	catabolic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:1djq, PDBe:1djq, PDBj:1djq
PDBsum	1djq
PubMed	10869173
UniProt	P16099\|DHTM_METME Trimethylamine dehydrogenase (Gene Name=tmd)

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