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Crystal structure of solute binding protein of ABC transporter in complex with P-hydroxybenzoic acid
Analyse Crystal structure of solute binding protein of ABC transporter in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EY3
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Twin-arginine translocation pathway signal
- UniProt
- Q13AR6
- Ligands
- PHB
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Twin-arginine translocation pathway signal | protein | 364 | 41% helix, 26% strand | Q13AR6 |
Ligands and binding sites
- PHB · P-hydroxybenzoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 4EY3 · Crystal structure of solute binding protein of ABC transporter in complex with… · 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 Q13AR6
- Elsewhere: RCSB PDB 4EY3 · PDBe 4EY3 · UniProt Q13AR6
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