Structure of PDB 2wyw Chain A

Receptor sequence
>2wywA (length=259) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MLTVDLSGKKALVMGVTNQRSLGFAIAAKLKEAGAEVALSYQAERLRPEA
EKLAEALGGALLFRADVTQDEELDALFAGVKEAFGGLDYLVHAIAFAPRE
AMEGRYIDTRRQDWLLALEVSAYSLVAVARRAEPLLREGGGIVTLTYYAS
EKVVPKYNVMAIAKAALEASVRYLAYELGPKGVRVNAISAGPVRTVAARS
IPGFTKMYDRVAQTAPLRRNITQEEVGNLGLFLLSPLASGITGEVVYVDA
GYHIMGMEL
3D structure
PDB2wyw 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.
ChainA
Resolution1.9 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 A V16 T17 S21 L22 Q42 D66 V67 A93 I94 A95 V120 L145 T146 K164 A190 P192 V193 T195 A197 V16 T17 S21 L22 Q42 D66 V67 A93 I94 A95 V120 L145 T146 K164 A190 P192 V193 T195 A197
BS02 TCL A A95 A97 Y147 Y157 A197 I201 F204 A95 A97 Y147 Y157 A197 I201 F204
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

View graph for
Biological Process
External links
PDB RCSB:2wyw, PDBe:2wyw, PDBj:2wyw
PDBsum2wyw
PubMed23027736
UniProtQ5SLI9

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