Research workbench
Structural basis for the negative regulation of bacterial stress response by rseb
Analyse Structural basis for the negative regulation of bacterial stress response by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3M4W
- Type
- protein
- Length
- 1,264 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AFX9, P0AFX7
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 284 | — | P0AFX9 |
| C | — | protein | 276 | — | P0AFX9 |
| D | — | protein | 269 | — | P0AFX9 |
| E, F | — | protein | 42 | — | P0AFX7 |
| G | — | protein | 36 | — | P0AFX7 |
| H | — | protein | 31 | — | P0AFX7 |
Compared structures
- 3M4W · Structural basis for the negative regulation of bacterial stress response by RseB · the same entry in another collection · chain H against H, TM-score 1.00
- P0AFX7 · AlphaFold monomer V2.0 prediction for anti-sigma-E factor rsea (P0AFX7) · a predicted model of the same protein · chain G against A, TM-score 0.51
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 P0AFX9
- Every structure of UniProt P0AFX7
- Elsewhere: RCSB PDB 3M4W · PDBe 3M4W · UniProt P0AFX9 · UniProt P0AFX7
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