Structure of PDB 2pd3 Chain C

Receptor sequence
>2pd3C (length=274) Species: 210 (Helicobacter pylori) [Search protein sequence]
GFLKGKKGLIVGVANNKSIAYGIAQSCFNQGATLAFTYLNESLEKRVRPI
AQELNSPYVYELDVSKEEHFKSLYNSVKKDLGSLDFIVHSVAFAPKEALE
GSLLETSKSAFNTAMEISVYSLIELTNTLKPLLNNGASVLTLSYLGSTKY
MAHYNVMGLAKAALESAVRYLAVDLGKHHIRVNALSAGPIRTLASSGIAD
FRMILKWNEINAPLRKNVSLEEVGNAGMYLLSSLSSGVSGEVHFVDAGYH
VMGMGAVEEKDNKATLLWDLHKEQ
3D structure
PDB2pd3 Crystal structure of the Helicobacter pylori enoyl-acyl carrier protein reductase in complex with hydroxydiphenyl ether compounds, triclosan and diclosan
ChainC
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y155 K162
Catalytic site (residue number reindexed from 1) Y154 K161
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 G13 A15 S19 I20 L40 D64 V65 S91 V92 A93 I118 L143 S144 Y145 K162 P190 I191 T193 A195 G12 A14 S18 I19 L39 D63 V64 S90 V91 A92 I117 L142 S143 Y144 K161 P189 I190 T192 A194
BS02 TCL C A93 F94 A95 L100 Y145 Y155 A195 F202 A92 F93 A94 L99 Y144 Y154 A194 F201
Gene Ontology
Molecular Function
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0030497 fatty acid elongation

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Molecular Function
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Biological Process
External links
PDB RCSB:2pd3, PDBe:2pd3, PDBj:2pd3
PDBsum2pd3
PubMed17879346
UniProtO24990|FABI_HELPY Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (Gene Name=fabI)

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