Research workbench
Trimeric structure of omp-PST1, the major porin from providencia stuartii
Analyse Trimeric structure of omp-PST1, the major porin from providencia stuartii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NXR
- Type
- protein
- Length
- 1,056 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E3U904
- Ligands
- CA, CL
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, B | — | protein | 352 | — | E3U904 |
Ligands and binding sites
- CA · Calcium ion · metal
- CL · Chloride ion · ion · chains A
- LDA · Lauryl dimethylamine-N-oxide · additive · 72 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NXR · Trimeric structure of Omp-Pst1, the major porin from Providencia stuartii · 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 E3U904
- Elsewhere: RCSB PDB 5NXR · PDBe 5NXR · UniProt E3U904
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