Research workbench
Structure of the amino acid ABC transporter, periplasmic amino acid- binding protein from coxiella burnetii.
Analyse Structure of the amino acid ABC transporter, periplasmic amino acid- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TQL
- Type
- protein
- Length
- 225 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginine-binding protein
- UniProt
- Q83E49
- Ligands
- ARG
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine-binding protein | protein | 225 | 37% helix, 25% strand | Q83E49 |
Ligands and binding sites
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 | 403 | 0.64 | 0.78 | 43 | ARG, IMD |
Modifications
Observed in the structure: 4 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 3TQL · Structure of the amino acid ABC transporter, periplasmic amino acid-binding protein from… · 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 Q83E49
- Elsewhere: RCSB PDB 3TQL · PDBe 3TQL · UniProt Q83E49
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