Research workbench
Hha-H-NS46 charge zipper complex
Analyse Hha-H-NS46 charge zipper complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MW2
- Type
- protein
- Length
- 155 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemolysin expression-modulating protein hha; DNA-binding protein H-ns
- UniProt
- P0ACE3, P0ACF8
- Pockets
- 3 · best druggability 0.72
Structure
solution nmr · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemolysin expression-modulating protein hha | protein | 67 | 61% helix, 0% strand | P0ACE3 |
| B, C | DNA-binding protein H-ns | protein | 44 | 77% helix, 0% strand | P0ACF8 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.72 | 0.94 | 27 | empty |
| 2 | 96 | 0.55 | 0.84 | 16 | empty |
| 3 | 64 | 0.33 | 0.76 | 13 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1640 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 471 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 466 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2MW2 · Hha-H-NS46 charge zipper complex · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACE3 · AlphaFold monomer V2.0 prediction for hemolysin expression-modulating protein hha (P0ACE3) · a predicted model of the same protein · chain A against A, TM-score 0.93
- P0ACF8 · AlphaFold monomer V2.0 prediction for DNA-binding protein H-ns (P0ACF8) · a predicted model of the same protein · chain B against A, TM-score 0.91
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 P0ACE3
- Every structure of UniProt P0ACF8
- Elsewhere: RCSB PDB 2MW2 · PDBe 2MW2 · UniProt P0ACE3 · UniProt P0ACF8
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