Research workbench
Multiple antibiotic resistance repressor, marr
Analyse Multiple antibiotic resistance repressor, marr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JGS
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multiple antibiotic resistance protein marr
- UniProt
- P27245
- Ligands
- SAL
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 62% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multiple antibiotic resistance protein marr | protein | 138 | 62% helix, 8% strand | P27245 |
Ligands and binding sites
- SAL · 2-hydroxybenzoic acid · ligand · 2 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.38 | 0.73 | 21 | empty |
Compared structures
- 1JGS · Multiple Antibiotic Resistance Repressor, MarR · the same entry in another collection · chain A against A, TM-score 1.00
- P27245 · AlphaFold monomer V2.0 prediction for multiple antibiotic resistance protein marr (P27245) · a predicted model of the same protein · chain A against A, TM-score 0.77
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 P27245
- Elsewhere: RCSB PDB 1JGS · PDBe 1JGS · UniProt P27245
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