Research workbench
Crystal structure of substrate-binding periplasmic protein (pbp) from ralstonia solanacearum
Analyse Crystal structure of substrate-binding periplasmic protein (pbp) from ralstonia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LOP
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Substrate binding periplasmic protein
- Ligands
- LEU, NI, MG, MN
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Substrate binding periplasmic protein | protein | 353 | 44% helix, 18% strand | — |
Ligands and binding sites
- LEU · Leucine · ligand · chains A
- NI · Nickel (II) ion · metal · 2 copies · chains A
- MG · Magnesium ion · metal · chains A
- MN · Manganese (II) ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3LOP · Crystal structure of substrate-binding periplasmic protein (Pbp) from Ralstonia… · 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
- Elsewhere: RCSB PDB 3LOP · PDBe 3LOP
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.