MolNFT v1 · #128041 · protein
Discovery, crystal structures and atomic force microscopy study of thioether ligated D,L-cyclic antimicrobial peptides against multidrug resistant pseudomonas aeruginosa
5NES: “Discovery, crystal structures and atomic force microscopy study of thioether ligated D,L-cyclic antimicrobial…”. X-ray diffraction, 3 ligands (8VH, ZDC, CA). MolNFT v1 #128041 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5NES
- Type
- protein
- Length
- 467 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A069Q9V4
- Ligands
- 8VH, ZDC, CA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 114 | — | A0A069Q9V4 |
| E | — | protein | 11 | — | — |
Ligands and binding sites
- 8VH · 1,3-dimethylbenzene · ligand · chains E
- ZDC · 3,7-anhydro-2,8-dideoxy-L-glycero-D-gluco-octonic acid · sugar · 4 copies · chains A, C, E, B, D
- CA · Calcium ion · metal · 8 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NES · Discovery, crystal structures and atomic force microscopy study of thioether ligated… · 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 A0A069Q9V4
- Elsewhere: RCSB PDB 5NES · PDBe 5NES · UniProt A0A069Q9V4
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