Research workbench
Lipid a secondary acyltransferase lpxm from acinetobacter baumannii with catalytic residue substitution (E127A)
Analyse Lipid a secondary acyltransferase lpxm from acinetobacter baumannii with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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.
| Volume (ų) | 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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