Structure of PDB 4dpl Chain B

Receptor sequence
>4dplB (length=354) Species: 273063 (Sulfurisphaera tokodaii str. 7) [Search protein sequence]
RTLKAAILGATGLVGIEYVRMLSNHPYIKPAYLAGKGSVGKPYGEVVRWQ
TVGQVPKEIADMEIKPTDPKLMDDVDIIFSPLPQGAAGPVEEQFAKEGFP
VISNSPDHRFDPDVPLLVPELNPHTISLIDEQRKRREWKGFIVTTPLCTA
QGAAIPLGAIFKDYKMDGAFITTIQSLSGAGYPGIPSLDVVDNILPLGDG
YDAKTIKEIFRILSEVKRNVDEPKLEDVSLAATTHRIATIHGHYEVLYVS
FKEETAAEKVKETLENFRGEPQDLKLPTAPSKPIIVMNEDTRPQVYFDRW
AGDIPGMSVVVGRLKQVNKRMIRLVSLIHNTVRGAAGGGILAAELLVEKG
YIEK
3D structure
PDB4dpl Structural Basis for a Bispecific NADP+ and CoA Binding Site in an Archaeal Malonyl-Coenzyme A Reductase.
ChainB
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.2.1.75: malonyl CoA reductase (malonate semialdehyde-forming).
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 NAP B G14 T16 G17 L18 V19 K41 G42 P86 L87 P88 N109 C153 G184 G186 Y187 N335 T336 G339 A340 G9 T11 G12 L13 V14 K36 G37 P81 L82 P83 N104 C148 G179 G181 Y182 N330 T331 G334 A335
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0004073 aspartate-semialdehyde dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046983 protein dimerization activity
GO:0050661 NADP binding
GO:0051287 NAD binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009086 methionine biosynthetic process
GO:0009088 threonine biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4dpl, PDBe:4dpl, PDBj:4dpl
PDBsum4dpl
PubMed23325803
UniProtQ96YK1|MCR_SULTO Malonyl-CoA reductase (Gene Name=mcr)

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