MolNFT v1 · #124722 · protein

Lipid a secondary acyltransferase lpxm from acinetobacter baumannii with catalytic residue substitution (E127A)

5KNK · Lipid a biosynthesis lauroyl acyltransferase: “Lipid a secondary acyltransferase lpxm from acinetobacter baumannii with catalytic residue substitution…”. X-ray diffraction, 2 ligands (11A, SO4), 3 pockets (best druggability 0.66).…

PDB: 5KNK
Type: protein
Length: 324 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipid a biosynthesis lauroyl acyltransferase
UniProt: S3TFW2
Ligands: 11A, SO4
Pockets: 3 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Lipid a biosynthesis lauroyl acyltransferase	protein	324	53% helix, 15% strand	S3TFW2

Ligands and binding sites

11A · Undecanoic acid · ligand · chains B
SO4 · Sulfate ion · ion · 4 copies · chains B
GOL · Glycerol · additive · 3 copies · chains B
LMT · Dodecyl-beta-D-maltoside · additive · 2 copies · chains B

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

Pockets

3 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	529	0.66	0.77	42	LMT
2	63	0.28	0.73	11	GOL
3	51	0.27	0.74	17	empty

Compared structures

5KNK · Lipid A secondary acyltransferase LpxM from Acinetobacter baumannii with catalytic… · 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 5KNK · PDBe 5KNK · UniProt S3TFW2

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