Research workbench
Crystal structure of a designed homodimeric variant T-A(L)A( L) of the tetracycline repressor
Analyse Crystal structure of a designed homodimeric variant T-A(L)A( L) of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XGD
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetracycline repressor protein class B from transposon TN10, tetracycline repressor…
- UniProt
- P04483, P0ACT4
- Ligands
- CL
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tetracycline repressor protein class B from transposon TN10, tetracycline repressor protein class D | protein | 194 | 71% helix, 0% strand | P04483, P0ACT4 |
Ligands and binding sites
- CL · Chloride ion · ion · 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 | 303 | 0.62 | 0.79 | 32 | empty |
Compared structures
- 2XGD · Crystal structure of a designed homodimeric variant T-A(L)A(L) of the tetracycline… · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACT4 · AlphaFold monomer V2.0 prediction for tetracycline repressor protein class D (P0ACT4) · a predicted model of the same protein · chain A against A, TM-score 0.95
- P04483 · AlphaFold monomer V2.0 prediction for tetracycline repressor protein class B from… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P04483
- Every structure of UniProt P0ACT4
- Elsewhere: RCSB PDB 2XGD · PDBe 2XGD · UniProt P04483 · UniProt P0ACT4
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