Structure of PDB 1djn Chain B

Receptor sequence
>1djnB (length=729) Species: 2327 (Methylophilus methylotrophus W3A1) [Search protein sequence]
ARDPKHDILFEPIQIGPKTLRNRFYQVPHCIGAGSDKPGFQSAHRSVKAE
GGWAALNTEYCSINPESDDTHRLSARIWDEGDVRNLKAMTDEVHKYGALA
GVELWYGGAHAPNMESRATPRGPSQYASEFETLSYCKEMDLSDIAQVQQF
YVDAAKRSRDAGFDIVYVYGAHSYLPLQFLNPYYNKRTDKYGGSLENRAR
FWLETLEKVKHAVGSDCAIATRFGVDTVYGPGQIEAEVDGQKFVEMADSL
VDMWDITIGDIAEWGEDAGPSRFYQQGHTIPWVKLVKQVSKKPVLGVGRY
TDPEKMIEIVTKGYADIIGCARPSIADPFLPQKVEQGRYDDIRVCIGCNV
CISRWEIGGPPMICTQNATAGEEYRRGWHPEKFRQTKNKDSVLIVGAGPS
GSEAARVLMESGYTVHLTDTAEKIGGHLNQVAALPGLGEWSYHRDYRETQ
ITKLLKKNKESQLALGQKPMTADDVLQYGADKVIIATGARWNTDGTNCLT
HDPIPGADASLPDQLTPEQVMDGKKKIGKRVVILNADTYFMAPSLAEKLA
TAGHEVTIVSGVHLANYMHFTLEYPNMMRRLHELHVEELGDHFCSRIEPG
RMEIYNIWGDGSKRTYRGPGVSPRDANTSHRWIEFDSLVLVTGRHSECTL
WNELKARESEWAENDIKGIYLIGDAEAPRLIADATFTGHRVAREIEEANP
QIAIPYKRETIAWGTPHMPGGNFKIEYKV
3D structure
PDB1djn Structural and biochemical characterization of recombinant wild type and a C30A mutant of trimethylamine dehydrogenase from methylophilus methylotrophus (sp. W(3)A(1)).
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C30 Y169 H172 Y174 R222 Y229 D267 V350
Catalytic site (residue number reindexed from 1) C30 Y169 H172 Y174 R222 Y229 D267 V350
Enzyme Commision number 1.5.8.2: trimethylamine dehydrogenase.
Interaction with ligand
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

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Molecular Function

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Biological Process
External links
PDB RCSB:1djn, PDBe:1djn, PDBj:1djn
PDBsum1djn
PubMed10869173
UniProtP16099|DHTM_METME Trimethylamine dehydrogenase (Gene Name=tmd)

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