Structure of PDB 4m89 Chain A

Receptor sequence

>4m89A (length=257) Species: 272831 (Neisseria meningitidis FAM18)

GFLQGKKILITGMISERSIAYGIAKACREQGAELAFTYVVDKLEERVRKM
AAELDSELVFRCDVASDDEINQVFADLGKHWDGLDGLVHSIGFAPKEALS
GDFLDSISREAFNTAHEISAYSLPALAKAARPMMRGRNSAIVALSYLGAV
RAIPNYNVMGMAKASLEAGIRFTAACLGKEGIRCNGISAGPIKTLAASGI
ADFGKLLGHVAAHNPLRRNVTIEEVGNTAAFLLSDLSSGITGEITYVDGG
YSINALS

3D structure

• PDB: 4m89 Crystal Structure of Enoyl-Acyl Carrier Protein Reductase (FabI) from Neisseria meningitidis in complex with NAD+ and Triclosan
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y157 K164
• Catalytic site (residue number reindexed from 1): Y156 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	A	G13 I15 S19 I20 V40 D64 V65 S91 I92 G93 I119 L145 S146 Y147 K164 A190 P192 I193 T195 A197	G12 I14 S18 I19 V39 D63 V64 S90 I91 G92 I118 L144 S145 Y146 K163 A189 P191 I192 T194 A196
BS02	TCL	A	G93 A95 L100 Y147 Y157 A197 I201 F204	G92 A94 L99 Y146 Y156 A196 I200 F203

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

External links

• PDB: RCSB:4m89, PDBe:4m89, PDBj:4m89
• PDBsum: 4m89
• UniProt: A1KVU8