Research workbench
Crystal structure of ABC transporter alpha-glycoside-binding mutant protein R356A in ligand free form
Analyse Crystal structure of ABC transporter alpha-glycoside-binding mutant protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JAL
- Type
- protein
- Length
- 416 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, periplasmic substrate-binding protein
- UniProt
- Q5SLD7
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC transporter, periplasmic substrate-binding protein | protein | 416 | 48% helix, 16% strand | Q5SLD7 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.55 | 0.75 | 47 | PEG |
Compared structures
- 6JAL · Crystal structure of ABC transporter alpha-glycoside-binding mutant protein R356A in… · 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 Q5SLD7
- Elsewhere: RCSB PDB 6JAL · PDBe 6JAL · UniProt Q5SLD7
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