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Crystal structure of peptidoglycan-associated lipoprotein from acinetobacter baumannii
Analyse Crystal structure of peptidoglycan-associated lipoprotein from acinetobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G4W
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidoglycan-associated lipoprotein
- UniProt
- F0QP95
- Ligands
- ALA, SO4
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidoglycan-associated lipoprotein | protein | 108 | 44% helix, 20% strand | F0QP95 |
Ligands and binding sites
- ALA · Alanine · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4G4W · Crystal structure of peptidoglycan-associated lipoprotein from Acinetobacter baumannii · the same entry in another collection · chain A against A, 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 F0QP95
- Elsewhere: RCSB PDB 4G4W · PDBe 4G4W · UniProt F0QP95
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