Structure of PDB 1tmo Chain A

Receptor sequence

>1tmoA (length=794) Species: 76854 (Shewanella massilia)

NEDEWLTTGSHFGAFKMKRKNGVIAEVKPFDLDKYPTDMINGIRGMVYNP
SRVRYPMVRLDFLLKGHKSNTHQRGDFRFVRVTWDKALTLFKHSLDEVQT
QYGPSGLHAGQTGWRATGQLHSSTSHMQRAVGMHGNYVKKIGDYSTGAGQ
TILPYVLGSTEVYAQGTSWPLILEHSDTIVLWSNDPYKNLQVGWNAETHE
SFAYLAQLKEKVKQGKIRVISIDPVVTKTQAYLGCEQLYVNPQTDVTLML
AIAHEMISKKLYDDKFIQGYSLGFEEFVPYVMGTKDGVAKTPEWAAPICG
VEAHVIRDLAKTLVKGRTQFMMGWCIQRQQHGEQPYWMAAVLATMIGQIG
LPGGGISYGHHYSSIGVPSSGAAAPGAFPRNLDENQKPLFDSSDFKGASS
TIPVARWIDAILEPGKTIDANGSKVVYPDIKMMIFSGNNPWNHHQDRNRM
KQAFHKLECVVTVDVNWTATCRFSDIVLPACTTYERNDIDVYGAYANRGI
LAMQKMVEPLFDSLSDFEIFTRFAAVLGKEKEYTRNMGEMEWLETLYNEC
KAANAGKFEMPDFATFWKQGYVHFGDGEVWTRHADFRNDPEINPLGTPSG
LIEIFSRKIDQFGYDDCKGHPTWMEKTERSHGGPGSDKHPIWLQSCHPDK
RLHSQMCESREYRETYAVNGREPVYISPVDAKARGIKDGDIVRVFNDRGQ
LLAGAVVSDNFPKGIVRIHEGAWYGPVGKDGSTEGGAEVGALCSYGDPNT
LTLDIGTSKLAQACSAYTCLVEFEKYQGKVPKVSSFDGPIEVEI

3D structure

• PDB: 1tmo Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T116 W118 D147 S149 T150 G363 Y366
• Catalytic site (residue number reindexed from 1): T112 W114 D143 S145 T146 G359 Y362
• Enzyme Commision number: 1.7.2.3: trimethylamine-N-oxide reductase.

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	2MD	A	W118 A120 S127 S149 N442 N443 H447 D468 S649 H651 H657 S658 Q659 N753 Y771	W114 A116 S123 S145 N438 N439 H443 D464 S645 H647 H653 S654 Q655 N749 Y767
BS02	2MD	A	S149 S187 K192 N193 V196 D227 D249 W328 C329 R332 H651 P652 H657	S145 S183 K188 N189 V192 D223 D245 W324 C325 R328 H647 P648 H653
BS03	2MO	A	W118 S149	W114 S145

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0030151 molybdenum ion binding
• GO:0043546 molybdopterin cofactor binding
• GO:0050626 trimethylamine-N-oxide reductase (cytochrome c) activity

Cellular Component

• GO:0042597 periplasmic space

External links

• PDB: RCSB:1tmo, PDBe:1tmo, PDBj:1tmo
• PDBsum: 1tmo
• PubMed: 9813128
• UniProt: O87948|TORA_SHEMA Trimethylamine-N-oxide reductase (Gene Name=torA)