Structure of PDB 5tf4 Chain C

Receptor sequence
>5tf4C (length=260) Species: 38323 (Bartonella henselae) [Search protein sequence]
GNGLLYGKRGLILGLANNRSIAWGIAKTASSAGAELAFTYQGEAMKKRVE
PLAEEVKGFVCGHCDVSDSASIDAVFNTIEKKWGKLDFLVHAIGFSDKEE
LSGRYVDISESNFMMTMNISVYSLTALTKRAEKLMSDGGSILTLTYYGAE
KVVPNYNVMGVAKAALEASVKYLAVDLGPKHIRVNAISAGPIKTLAASGI
GDFRYILKWNEYNAPLRRTVTIEEVGDSALYLLSDLSRSVTGEVHHVDSG
YNIIGMKAVD
3D structure
PDB5tf4 Crystal structure of enoyl-(acyl carrier protein) reductase from Bartonella henselae in complext with NAD
ChainC
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T148 Y159 M162 K166
Catalytic site (residue number reindexed from 1) T145 Y156 M159 K163
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 C G17 A19 S23 I24 Q44 D68 V69 A95 I96 I122 L147 T148 K166 A192 P194 I195 T197 A199 A200 G14 A16 S20 I21 Q41 D65 V66 A92 I93 I119 L144 T145 K163 A189 P191 I192 T194 A196 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5tf4, PDBe:5tf4, PDBj:5tf4
PDBsum5tf4
PubMed
UniProtA0A0H3M2Q2

[Back to BioLiP]