Research workbench
Crystal structure of D-allose binding protein from escherichia COLI
Analyse Crystal structure of D-allose binding protein from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RPJ
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (precursor of periplasmic sugar receptor)
- UniProt
- P39265
- Ligands
- ALL, ZN, SO4
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (precursor of periplasmic sugar receptor) | protein | 288 | 45% helix, 24% strand | P39265 |
Ligands and binding sites
- ALL · beta-D-allopyranose · ligand · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1RPJ · Crystal structure of D-allose binding protein from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
- P39265 · AlphaFold monomer V2.0 prediction for D-allose-binding periplasmic protein (P39265) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P39265
- Elsewhere: RCSB PDB 1RPJ · PDBe 1RPJ · UniProt P39265
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