Structure of PDB 5ocs Chain A

Receptor sequence
>5ocsA (length=369) Species: 119219 (Cupriavidus metallidurans) [Search protein sequence]
MPHLFDPYRIGNLELANRIAIAPMCQYSAQEGNATDWHMIHLGQMALSGA
GLLIIEATAVSPEGRITPTDLGLYNDANEAALGRVLGAVRNHSPIAVTIQ
LAHAGRKASSEAPWDGGGQIRPDQPRGWQTFAPSAVPHAAGEVPPAALDK
AGMKKIRDDFVAAAKRAARLGIEGIEVHGAHGYLLHQFLSPIANHRTDEY
GGSLENRMRFPLEVFDAVREAFPAERPVWMRVSATDWVPNGWDIEGTIAL
SHELKARGSAAVHVSTGGVSPQQAIKIGPGYQVPYAQRVKAEVGLPTMAV
GLITEAEQAEAIIANNEADIISIARAMLYDPRWPWHAAAKLGASVNAPKQ
YWRSQPRGLEKLFKDAHFG
3D structure
PDB5ocs Structural investigation into the C-terminal extension of the ene-reductase from Ralstonia (Cupriavidus) metallidurans.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C25 H178 H181 Y183 R231 P239
Catalytic site (residue number reindexed from 1) C25 H178 H181 Y183 R231 P239
Enzyme Commision number 1.6.99.1: NADPH 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)		 Binding affinity
BS01 FMN A P23 M24 C25 A57 Q100 H178 H181 R231 V300 G301 L302 A324 R325 P23 M24 C25 A57 Q100 H178 H181 R231 V300 G301 L302 A324 R325
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003959 NADPH dehydrogenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding

View graph for
Molecular Function
External links
PDB RCSB:5ocs, PDBe:5ocs, PDBj:5ocs
PDBsum5ocs
PubMed28833623
UniProtQ1LDQ5

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