Research workbench
The marr-family repressor mexr in complex with its antirepressor armr
Analyse The marr-family repressor mexr in complex with its antirepressor armr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ECH
- Type
- protein
- Length
- 288 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug resistance operon repressor; 25-mer fragment of protein armr
- UniProt
- P52003, Q9HXS2
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 3 distinct chains · 68% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug resistance operon repressor | protein | 129 | 71% helix, 3% strand | P52003 |
| B | Multidrug resistance operon repressor | protein | 135 | 65% helix, 9% strand | P52003 |
| C | 25-mer fragment of protein armr | protein | 24 | 71% helix, 0% strand | Q9HXS2 |
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 | 309 | 0.53 | 0.74 | 47 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2000 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 984 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 893 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3ECH · The MarR-family repressor MexR in complex with its antirepressor ArmR · the same entry in another collection · chain A against A, TM-score 1.00
- P52003 · AlphaFold monomer V2.0 prediction for multidrug resistance operon repressor (P52003) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 P52003
- Every structure of UniProt Q9HXS2
- Elsewhere: RCSB PDB 3ECH · PDBe 3ECH · UniProt P52003 · UniProt Q9HXS2
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