Research workbench
Methionine aporepressor mutant (Q44K) complexed to half of the consensus operator sequence
Analyse Methionine aporepressor mutant (Q44K) complexed to half of the consensus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MJM
- Type
- protein + DNA
- Length
- 228 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Half consensus DNA operator duplex; Methionine repressor
- UniProt
- P0A8U6
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | Half consensus DNA operator duplex | dna | 10 | — | — |
| A, B | Methionine repressor | protein | 104 | 40% helix, 13% strand | P0A8U6 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.39 | 0.75 | 24 | empty |
| 2 | 53 | 0.24 | 0.72 | 14 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1764 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 439 Ų buried · 46 hydrogen bonds · nucleic-nucleic
- D–A · 298 Ų buried · 7 hydrogen bonds · protein-nucleic
- C–B · 266 Ų buried · 5 hydrogen bonds · protein-nucleic
- C–A · 229 Ų buried · 4 hydrogen bonds · protein-nucleic
Compared structures
- 1MJM · Methionine aporepressor mutant (Q44K) complexed to half of the consensus operator sequence · the same entry in another collection · chain C against C, TM-score 1.00
- P0A8U6 · AlphaFold monomer V2.0 prediction for met repressor (P0A8U6) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P0A8U6
- Elsewhere: RCSB PDB 1MJM · PDBe 1MJM · UniProt P0A8U6
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