Structure of PDB 5mjk Chain A

Receptor sequence
>5mjkA (length=302) Species: 1359 (Lactococcus cremoris) [Search protein sequence]
KYDVVIIGSGPAGMTAAMYTARSEMKTLLLERGVPGGQMNNTAEIENYPG
YETIMGPELSMKMAEPLEGLGVENAYGFVTGIEDHGDYKKIITEDDEFIT
KSIIIATGANHRKLEIPGEEEYGARGVSYCAVCDGAFFRNQEILVIGGGD
SAVEEALYLTRFGQSVTIMHRRDKLRAQEIIQQRAFKEEKINFIWDSVPM
EIKGDDKKIQSVVYKNVKTGEVTEKAFGGIFIYVGLDPVAEFVSDLGITD
EAGWIITDDHMRTNIPGIFAVGDVRQKDFRQITTAVGDGAQAAQEAYKFV
VE
3D structure
PDB5mjk The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V38 P39 M43 E48 C134 C137 D138
Catalytic site (residue number reindexed from 1) V34 P35 M39 E44 C130 C133 D134
Enzyme Commision number 1.8.1.9: thioredoxin-disulfide 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 FAD A G12 G14 P15 A16 E35 R36 G41 Q42 T46 N51 G81 V83 T111 G112 C137 V243 F246 G276 D277 Q285 I286 G8 G10 P11 A12 E31 R32 G37 Q38 T42 N47 G77 V79 T107 G108 C133 V239 F242 G272 D273 Q281 I282
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004791 thioredoxin-disulfide reductase (NADPH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0019430 removal of superoxide radicals
GO:0045454 cell redox homeostasis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5mjk, PDBe:5mjk, PDBj:5mjk
PDBsum5mjk
PubMed28397795
UniProtA2RLJ5

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