Structure of PDB 3i3a Chain B

Receptor sequence
>3i3aB (length=259) Species: 173 (Leptospira interrogans) [Search protein sequence]
MKIHPTAIIDPKAELHESVEVGPYSIIEGNVSIQEGTIIEGHVKICAGSE
IGKFNRFHQGAVIGVMPQDLGFNQQLLTKTVIGDHNIFREYSNIHKGTKE
DSPTVIGNKNYFMGNSHVGHDCILGNNNILTHGAVLAGHVTLGNFAFISG
LVAVHQFCFVGDYSMVAGLAKVVQDVPPYSTVDGNPSTVVGLNSVGMKRA
GFSPEVRNAIKHAYKVIYHSGISTRKALDELEASGNLIEQVKYIIKFFRD
SDRGVTNHR
3D structure
PDB3i3a Structural basis for the sugar nucleotide and acyl-chain selectivity of Leptospira interrogans LpxA.
ChainB
Resolution2.12 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) H120 D121 G138
Catalytic site (residue number reindexed from 1) H120 D121 G138
Enzyme Commision number 2.3.1.129: acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase.
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 S2N B Q68 H117 V135 A137 A153 H155 Q156 R253 Q68 H117 V135 A137 A153 H155 Q156 R253
Gene Ontology
Molecular Function
GO:0008780 acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity
GO:0016746 acyltransferase activity
Biological Process
GO:0008610 lipid biosynthetic process
GO:0009245 lipid A biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3i3a, PDBe:3i3a, PDBj:3i3a
PDBsum3i3a
PubMed19456129
UniProtQ8EZA6

[Back to BioLiP]