Structure of PDB 2wyv Chain D

Receptor sequence
>2wyvD (length=257) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MLTVDLSGKKALVMGVTNQRSLGFAIAAKLKEAGAEVALSYQAERLRPEA
EKLAEALGGALLFRADVTQDEELDALFAGVKEAFGGLDYLVHAIAFAPRE
AMEGRYIDTRRQDWLLALEVSAYSLVAVARRAEPLLREGGGIVTLTYYAS
EKVVPKYNVMAIAKAALEASVRYLAYELGPKGVRVNAISAGPVRTVAARS
IPGFTKMYDRVAQTAPLRRNITQEEVGNLGLFLLSPLASGITGEVVYVDA
GYHIMGM
3D structure
PDB2wyv High-resolution structures of Thermus thermophilus enoyl-acyl carrier protein reductase in the apo form, in complex with NAD+ and in complex with NAD+ and triclosan.
ChainD
Resolution1.86 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S21 Y147 Y157 M160 K164
Catalytic site (residue number reindexed from 1) S21 Y147 Y157 M160 K164
Enzyme Commision number 1.3.1.9: enoyl-[acyl-carrier-protein] reductase (NADH).
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 G15 V16 T17 S21 L22 Q42 D66 V67 A93 I94 A95 V120 L145 T146 K164 A190 P192 V193 T195 A197 G15 V16 T17 S21 L22 Q42 D66 V67 A93 I94 A95 V120 L145 T146 K164 A190 P192 V193 T195 A197
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2wyv, PDBe:2wyv, PDBj:2wyv
PDBsum2wyv
PubMed23027736
UniProtQ5SLI9

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