Structure of PDB 3r3s Chain D

Receptor sequence
>3r3sD (length=292) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence]
HLYDPTTQYYTGEYPKQKQPAPGVQAKMTPVPDCGEKSYVGSGRLKDRKA
LVTGGDSGIGRAAAIAYAREGADVAINYLPAEEEDAQQVKALIEECGRKA
VLLPGDLSDESFARSLVHKAREALGGLDILALVAGKQTAIPEIKDLTSEQ
FQQTFAVNVFALFWITQEAIPLLPKGASIITTSSIQAYQPSPHLLDYAAT
KAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTALQISGGQTQDKIPQFGQ
QTPMKRAGQPAELAPVYVYLASQESSYVTAEVHGVCGGEHLG
3D structure
PDB3r3s Structure of the YghA Oxidoreductase from Salmonella enterica
ChainD
Resolution1.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G60 S186 L196 Y199 K203 Q244
Catalytic site (residue number reindexed from 1) G58 S184 L194 Y197 K201 Q242
Enzyme Commision number ?
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 NAD D D58 S59 G60 I61 L81 E84 D108 L109 V135 A136 G137 V159 S186 Y199 K203 P229 G230 P231 I232 T234 L236 Q237 D56 S57 G58 I59 L79 E82 D106 L107 V133 A134 G135 V157 S184 Y197 K201 P227 G228 P229 I230 T232 L234 Q235
BS02 MG D D58 S59 E84 D56 S57 E82
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:3r3s, PDBe:3r3s, PDBj:3r3s
PDBsum3r3s
PubMed
UniProtQ8ZM09

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