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Lipid a secondary acyltransferase lpxm from acinetobacter baumannii

Analyse Lipid a secondary acyltransferase lpxm from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KN7
Type: protein
Length: 319 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipid a biosynthesis lauroyl acyltransferase
UniProt: S3TFW2
Ligands: NA, SO4, PO4
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Lipid a biosynthesis lauroyl acyltransferase	protein	319	55% helix, 16% strand	S3TFW2

Ligands and binding sites

NA · Sodium ion · metal · 3 copies · chains B
SO4 · Sulfate ion · ion · 3 copies · chains B
PO4 · Phosphate ion · ion · chains B
GOL · Glycerol · additive · 8 copies · chains B
LMT · Dodecyl-beta-D-maltoside · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	505	0.69	0.79	45	GOL, LMT
2	60	0.30	0.74	16	GOL

Compared structures

5KN7 · Lipid A secondary acyltransferase LpxM from Acinetobacter baumannii · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt S3TFW2
Elsewhere: RCSB PDB 5KN7 · PDBe 5KN7 · UniProt S3TFW2

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